<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Anisotropic Terahertz Microscopy of Lysozyme in Different CrystalLattice Systems</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">02/2021</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.cell.com/biophysj/fulltext/S0006-3495(20)31879-8</style></url></web-urls></urls><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Long-range vibrational modes of proteins at terahertz (THz) frequencies havebeen associated with protein function and allosteric control. The characteriza-tion of these motions has been challenging due to energy overlap with waterabsorption and a large vibrational density of states. Recently it has been demon-strated both experimentally and theoretically that vibrational bands can be iso-lated using stationary sample anisotropic terahertz microscopy (SSTAM) fororiented samples, typically realized using protein crystals [1, 2]. In those earlymeasurements, inhibitor binding contrast was demonstrated for high symmetrytetragonal crystals. While high symmetry crystals are ideal for structural deter-minations, they can limit the types of vibrations observable in the ATM mea-surements. Here we show a survey of ATM measurements of triclinic,monoclinic and tetragonal crystals, demonstrating the unique signaturesobservable for the different symmetry groups, leading to a more completedetermination of the vibrational hot spots that may contribute to enzymatic ef-ficiency. The SSATM spectra indicate the presence of conserved vibrationalmodes near 40 cm&lt;sup&gt;-1&lt;/sup&gt; and 55 cm&lt;sup&gt;-1&lt;/sup&gt; for CEWL in triclinic, monoclinic and tetrag-onal lattice systems respectively. For CEWL in the monoclinic lattice system, aprominent band at 20cm1was consistently observed in the SSATM spectrabut not in the triclinic or tetragonal systems. The conserved bands may repre-sent vibrational modes that are unperturbed by crystal contact forces while thedifferences may be related to unique molecular orientation in different crystalsystems.&lt;/p&gt;

&lt;p&gt;&lt;br /&gt;
&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;1.Niessen, K., Y. Deng, and A.G. Markelz,&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;Near-field THz micropo-&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;larimetry.&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;Opt Express, 2019.&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;27&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;(20): p. 28036-28047.&lt;/span&gt;&lt;/p&gt;

&lt;p&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;2.Romo, T.D., A.&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;Grossfield, and A.G. Markelz&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;Persistent Protein Motions in a Rugged&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;Energy Landscape Revealed by Normal Mode Ensemble Analysis&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;. Accepted&lt;/span&gt;&lt;span dir=&quot;ltr&quot; style=&quot;font-family:serif; font-size:13.2837px&quot;&gt;Journal of Chemical Information and Modeling, 2020.&lt;/span&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Niessen, K. A.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Near-Field Stationary Sample Terahertz Spectroscopic Polarimetry for Biomolecular Structural Dynamics Determination</style></title><secondary-title><style face="normal" font="default" size="100%">ACS Photonics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">02/2021</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://pubs.acs.org/doi/abs/10.1021/acsphotonics.0c01876</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">8</style></volume><pages><style face="normal" font="default" size="100%">658-668</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;THz polarimetry on environmentally sensitive and microscopic samples can provide unique insight into underlying mechanisms of complex phenomena. For example, near-field THz anisotropic absorption successfully isolated protein structural vibrations which are connected to biological function. However, to determine how these vibrations impact function requires high throughput measurements of these complex systems, which is challenged by the need for near field detection, sample environmental control and full polarization variation. Stationary sample anisotropic terahertz spectroscopy (SSATS) and near-field stationary sample anisotropic terahertz microscopy (SSATM) have been proposed using synchronous control of THz and electro optic probe polarizations along an iso-response curve. Here we realize these techniques through robust control and calibration of the THz and NIR polarization states. Both methods rapidly measure the linear dichroism in the far field and near field. Validation measurements using standard birefringent sucrose single crystals found the crystal orientation can be determined by scanning the reference polarization and the synchronous pump–probe polarization settings can be optimized to eliminate artifacts. SSATM is then used to determine spectral reproducibility and dehydration effects for a series of chicken egg white lysozyme samples. Reproducible anisotropic absorbance bands are found at about 30, 44, 55, and 62 cm&lt;sup&gt;–1&lt;/sup&gt;. These bands initially sharpen with slow dehydration, similar to the increase in resolution achieved in X-ray crystallographic protein structure determination. The SSATM technique confirms the reliability of anisotropic absorption characterization of protein intramolecular vibrations and opens an avenue for rapid determination of how these long-range dynamics affect biological function.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><section><style face="normal" font="default" size="100%">658</style></section></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">A. Davie</style></author><author><style face="normal" font="default" size="100%">F. Vandrevala</style></author><author><style face="normal" font="default" size="100%">S. Dampf</style></author><author><style face="normal" font="default" size="100%">Y. Deng</style></author><author><style face="normal" font="default" size="100%">D. K. George</style></author><author><style face="normal" font="default" size="100%">E. D. Sylvester</style></author><author><style face="normal" font="default" size="100%">T. Korter</style></author><author><style face="normal" font="default" size="100%">E. Einarsson</style></author><author><style face="normal" font="default" size="100%">J. B. Benedict</style></author><author><style face="normal" font="default" size="100%">A. G. Markelz</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Phonon Kinetics of Fructose at the Melting Transition</style></title><secondary-title><style face="normal" font="default" size="100%">J. Phys. Chem. C</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2021</style></year></dates><volume><style face="normal" font="default" size="100%">125</style></volume><pages><style face="normal" font="default" size="100%">12269-12276</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;Terahertz time domain spectroscopy (THz TDS) is used to measure the melting kinetics of fructose molecular crystals. Combining single-crystal anisotropy measurements with density functional calculations, we assign the phonon frequencies and interrogate how specific phonons behave with melting. While nearly all the low-frequency phonons continuously red-shift with heating and melting, the lowest-energy phonon polarized along the c-axis blue-shifts at the melting temperature, suggesting an initial structural change immediately before melting. We find that the kinetics follow a 3D growth model with large activation energies, consistent with previous differential scanning calorimetry (DSC) measurements. The large activation energies indicate that multiple H-bonds must break collectively for the transition. The results suggest the generality of the kinetics for molecular crystals and that THz TDS with picosecond resolution could be used to measure ultrafast kinetics.&lt;/p&gt;

&lt;p&gt;&amp;nbsp;&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">22</style></issue><section><style face="normal" font="default" size="100%">12269</style></section></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">Crossen, K.</style></author><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Lechno-Yossef, S.</style></author><author><style face="normal" font="default" size="100%">Kerfeld, C.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Evidence of Intramolecular Structural Stabilization in Light Activated State of Orange Carotenoid Protein</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">118</style></volume><pages><style face="normal" font="default" size="100%">208A-208A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;Orange carotenoid protein (OCP) controls efficiency of the light harvesting antenna, the phycobilisome (PBS), in diverse cyanobacteria and prevents oxidative damage. It is the only known photoactive protein that uses a carotenoid, canthaxanthin, as its chromophore. The structure of OCP consists of two globular domains, connected by an unstructured loop, that forms a hydrophobic pocket for the carotenoid. In low light, canthaxanthin bound OCP is inactive and appears orange. Illumination by strong light results in an active state that interacts with the PBS to induce fluorescence quenching, a red appearance and conformational changes that include a 12Å shift by canthaxanthin into the N-terminal domain. Terahertz (THz) dynamical transition measurements and anisotropic terahertz microscopy are used to measure the intramolecular structural dynamics in the inactive and active states, which can be induced by photoexcitation or chaotropic salts. The measurements indicate that the active state has a decrease in structural flexibility, which may be related to enhanced interactions with the PBS.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000513023201290</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: KK8YX&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 0&lt;br/&gt;McKinney, Jeffrey A. Sharma, Akansha Crossen, Kimberly Deng, Yanting George, Deepu K. Lechno-Yossef, Sigal Kerfeld, Cheryl Markelz, Andrea G.&lt;br/&gt;64th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2020&lt;br/&gt;San Diego, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;NSFNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; DOEUnited States Department of Energy (DOE) [DE-SC0016317]; NIH STTRUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USA [R41 GM125486]&lt;br/&gt;This work is supported by NSF grants DBI 1556359 and MCB 1616529, DOE grant DE-SC0016317 and NIH STTR R41 GM125486.&lt;br/&gt;&lt;br/&gt;1&lt;br/&gt;2&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086</style></notes><auth-address><style face="normal" font="default" size="100%">[McKinney, Jeffrey A.|Sharma, Akansha|Crossen, Kimberly|Deng, Yanting|George, Deepu K.|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Lechno-Yossef, Sigal] Michigan State Univ, Dept Phys, E Lansing, MI 48824 USA. [Kerfeld, Cheryl] Michigan State Univ, Lawrence Berkeley Natl Lab LBNL, E Lansing, MI 48824 USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Richard, J.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Long Range Correlated Motions of TIM and their Possible Influence on Enzyme Function</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">118</style></volume><pages><style face="normal" font="default" size="100%">207A-207A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;The alpha-beta barrel structure of triosephosphate isomerase (TIM) is possibly the most common among enzymes. In the case of TIM, structural dynamics are known to be essential to function. In particular the stabilization of the binding pocket by a phosphodianion “handle” of the substrate and the closing of catalytic site loops 6 and 7 over the substrate. Loop 6 moves by as much as 7 Angstroms with binding. Recently a mutant survey for human TIM (hsTIM) found kcat can change significantly for a single mutation distant from the catalytic site. Crystallographic measurements find no structural change with the mutation, suggesting a dynamical mechanism for the allosteric effect. Here we use Stationary Sample Anisotropic Terahertz Microscopy (SSATM) to measure the long-range intramolecular vibrations and determine if specific vibrations couple the allosteric and catalytic sites. SSATM isolated protein long-range structural vibrations based on the dominant displacement direction [1-4]. We examine if specific vibrational bands are associate with loop 6 and loop 7 flexibility.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000513023201285</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: KK8YX&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 4&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Niessen K.A. M.Y., 2017, BIOPHYS J, DOI [10.1016/j.bpj.2016.12.049.3., DOI 10.1016/J.BPJ.2016.12.049.3]&lt;br/&gt;     Niessen K, 2019, OPT EXPRESS, V27, P28036, DOI 10.1364/OE.27.028036&lt;br/&gt;     Niessen KA, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08926-3&lt;br/&gt;McKinney, Jeffrey A. Deng, Yanting George, Deepu K. Richard, John Markelz, Andrea G.&lt;br/&gt;64th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2020&lt;br/&gt;San Diego, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;NSFNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; DOEUnited States Department of Energy (DOE) [DE-SC0016317]; NIH STTRUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USA [R41 GM125486.1]&lt;br/&gt;This work is supported by NSF grants DBI 1556359 and MCB 1616529, DOE grant DE-SC0016317 and NIH STTR R41 GM125486.1.&lt;br/&gt;&lt;br/&gt;1&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086</style></notes><auth-address><style face="normal" font="default" size="100%">[McKinney, Jeffrey A.|Deng, Yanting|George, Deepu K.|Markelz, Andrea G.] SUNY Buffalo, Univ Buffalo, Phys, Buffalo, NY USA. [Richard, John] SUNY Buffalo, Univ Buffalo, Chem, Buffalo, NY USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>10</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">George, D.</style></author><author><style face="normal" font="default" size="100%">Lechno-Yossef, S.</style></author><author><style face="normal" font="default" size="100%">Kerfeld, C.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stabilization of Terahertz Vibrational Modes in Illuminated Orange Carotenoid Protein Crystals</style></title><secondary-title><style face="normal" font="default" size="100%">2020 45th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2020</style></year></dates><pub-location><style face="normal" font="default" size="100%">Buffalo, NY</style></pub-location><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;Orange carotenoid protein (OCP) controls efficiency of the phycobilisome (PBS), the light harvesting antenna in cyanobacteria, to prevent oxidative damage. The OCP switches from resting state to photo protective state with intense blue light illumination. Questions persist as to why OCPR interaction increases with the PBS over that with the OCPO. Here we examine the role of long-range intramolecular vibrations within OCP. Using Stationary Sample Anisotropic Terahertz Microscopy (SSATM) we measure changes in the intramolecular vibrations with photo switching. We report the first observation of switching in the intramolecular vibrations with photoexcitation. Results suggest that there is a stiffening of the molecule in the photo protective state. This increase in structural stability may enhance the interaction with the PBS change in OCP interaction with PBS. In low light, carotenoid bound OCP appears orange (OCP &lt;sup&gt;o&lt;/sup&gt; ) and is inactive. Illumination by strong light converts OCP to the active, red (OCPR) state, which interacts with the PBS. A comparison of anisotropic THz microscopy measurements of dark adapted (OCP &lt;sup&gt;o&lt;/sup&gt; ) and illuminated OCP crystals indicate differences in their vibrational modes that may be important for OCP-PBS interactions.&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>10</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Y. Deng</style></author><author><style face="normal" font="default" size="100%">K. Niessen</style></author><author><style face="normal" font="default" size="100%">A. Markelz</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Angular Distortion Removal of THz Anisotropic Dichroism Microscope</style></title><secondary-title><style face="normal" font="default" size="100%">2019 44th International Conference on Infrared, Millimeter, and Terahertz Waves</style></secondary-title><short-title><style face="normal" font="default" size="100%">2019 44th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">absorption</style></keyword><keyword><style  face="normal" font="default" size="100%">angular distortion removal</style></keyword><keyword><style  face="normal" font="default" size="100%">Biomedical measurement</style></keyword><keyword><style  face="normal" font="default" size="100%">continuous iso-response curve</style></keyword><keyword><style  face="normal" font="default" size="100%">detection light polarizations</style></keyword><keyword><style  face="normal" font="default" size="100%">discontinuous iso-response angle pairs</style></keyword><keyword><style  face="normal" font="default" size="100%">Distortion</style></keyword><keyword><style  face="normal" font="default" size="100%">light polarisation</style></keyword><keyword><style  face="normal" font="default" size="100%">material characterization</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">rapid anisotropic terahertz spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">relative polarizations</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">stationary sample</style></keyword><keyword><style  face="normal" font="default" size="100%">terahertz spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">terahertz wave spectra</style></keyword><keyword><style  face="normal" font="default" size="100%">THz anisotropic dichroism microscope</style></keyword><keyword><style  face="normal" font="default" size="100%">vibrations</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2019</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://ieeexplore.ieee.org/document/8873793</style></url></web-urls></urls><pub-location><style face="normal" font="default" size="100%">Paris, France</style></pub-location><pages><style face="normal" font="default" size="100%">1 - 2</style></pages><isbn><style face="normal" font="default" size="100%">2162-2035</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We have developed a stationary sample THz anisotropic dichroism microscope as a powerful tool for material characterization. The key innovation is the use of an iso-response curve defined by the terahertz and detection light polarizations. Here we show that following a continuous iso-response curve introduces angular distortion in the spectrum, and this distortion can be eliminated by using a discontinuous iso-response angle pairs avoiding large gradient regions. Employing this additional constraint on the relative polarizations provides a convenient technique for rapid anisotropic terahertz spectroscopy.&lt;/p&gt;</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>10</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Anisotropic Terahertz Microscopy of Protein Collective Vibrations: Crystal Symmetry and Hydration Dependence</style></title><secondary-title><style face="normal" font="default" size="100%">2019 44th International Conference on Infrared, Millimeter, and Terahertz Waves</style></secondary-title><tertiary-title><style face="normal" font="default" size="100%">International Conference on Infrared Millimeter and Terahertz Waves</style></tertiary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><publisher><style face="normal" font="default" size="100%">Ieee</style></publisher><pub-location><style face="normal" font="default" size="100%">New York</style></pub-location><isbn><style face="normal" font="default" size="100%">978-1-5386-8285-2</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A stationary sample anisotropic terahertz microscopy technique is used to characterize the intramolecular vibrations for lysozyme. Tetragonal and triclinic crystals are compared. We find excellent reproducibility within a single crystal symmetry group. Several resonant bands are present for both symmetry groups, indicating they originate with the intramolecular vibrations and not crystal lattice phonons. Bands become more pronounced and higher frequency resonant bands begin to emerge with slight dehydration.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000591783800033</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BQ4OX&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 4&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Legrand L, 2002, ACTA CRYSTALLOGR D, V58, P1564, DOI 10.1107/S0907444902014403&lt;br/&gt;     Niessen KA, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08926-3&lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;McKinney, Jeffrey Deng, Yanting Sharma, Akansha George, D. K. Markelz, A. G.&lt;br/&gt;Irmmw-thz&lt;br/&gt;Proceedings Paper&lt;br/&gt;44th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)&lt;br/&gt;Sep 01-06, 2019&lt;br/&gt;Paris, FRANCE&lt;br/&gt;Lytid, TYDEX, Swiss Terahertz, Fondat Maison Chimie, CNRS, Lab Physique ENS, Li2S, LUNA, MenloSystems, ENS, PSL Univ Paris, FYLA, ADVANTEST, Springer Nature, Soc Francaise Physique, Sorbonne Univ, Int Soc Infrared Millimeter &amp; Terahertz Waves, IEEE, GDR NANO THz MIR&lt;br/&gt;NSFNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; DOEUnited States Department of Energy (DOE) [DE-SC0016317]; NIHUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USA [STTR R41 GM125486]&lt;br/&gt;This work is supported by NSF grants DBI 1556359 and MCB 1616529, DOE grant DE-SC0016317 and NIH STTR R41 GM125486.&lt;br/&gt;345 e 47th st, new york, ny 10017 usa&lt;br/&gt;2162-2027</style></notes><auth-address><style face="normal" font="default" size="100%">[McKinney, Jeffrey|Deng, Yanting|Sharma, Akansha|George, D. K.|Markelz, A. G.] Univ Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;McKinney, J (corresponding author), Univ Buffalo, Dept Phys, Buffalo, NY 14260 USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Davie, Alex</style></author><author><style face="normal" font="default" size="100%">Vandrevala, Farah</style></author><author><style face="normal" font="default" size="100%">Deng, Yanting</style></author><author><style face="normal" font="default" size="100%">George, D.</style></author><author><style face="normal" font="default" size="100%">Sylvester, Eric D.</style></author><author><style face="normal" font="default" size="100%">Korter, T.</style></author><author><style face="normal" font="default" size="100%">Einarsson, E.</style></author><author><style face="normal" font="default" size="100%">Benedict, Jason B.</style></author><author><style face="normal" font="default" size="100%">Markelz, Andrea</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Blue Shift of a Molecular Crystal Phonon at the Solid to Liquid Phase Transition</style></title><secondary-title><style face="normal" font="default" size="100%">Bulletin of the American Physical Society</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><volume><style face="normal" font="default" size="100%">2019</style></volume><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Deuteration and Inhibitor Binding Dependence of Protein Collective Vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">116</style></volume><pages><style face="normal" font="default" size="100%">488A-488A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000460779802452</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 2&lt;br/&gt;Cited References: &lt;br/&gt;     Mahajan S, 2015, ARCH BIOCHEM BIOPHYS, V567, P59, DOI 10.1016/j.abb.2014.12.020&lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;Deng, Yanting Mckinney, Jeffrey Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Mckinney, Jeffrey|Markelz, Andrea] SUNY Buffalo, Phys, Buffalo, NY USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">George, D.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Effect of Crystal Contact Forces on the Protein Global Motions</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">116</style></volume><pages><style face="normal" font="default" size="100%">489A-489A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000460779802457</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 1&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;McKinney, Jeffrey A. Deng, Yanting George, Deepu Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[McKinney, Jeffrey A.|Deng, Yanting|George, Deepu|Markelz, Andrea] Univ Buffalo, Phys, Buffalo, NY USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Niessen, K.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Near-field THz micropolarimetry</style></title><secondary-title><style face="normal" font="default" size="100%">Optics Express</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Opt. Express</style></alt-title><short-title><style face="normal" font="default" size="100%">Opt. ExpressOpt. Express</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">binding</style></keyword><keyword><style  face="normal" font="default" size="100%">conductivity</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">modes</style></keyword><keyword><style  face="normal" font="default" size="100%">Optics</style></keyword><keyword><style  face="normal" font="default" size="100%">polarization modulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Terahertz</style></keyword><keyword><style  face="normal" font="default" size="100%">time-domain spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">wse2</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Sep</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">20</style></number><volume><style face="normal" font="default" size="100%">27</style></volume><pages><style face="normal" font="default" size="100%">28036-28047</style></pages><isbn><style face="normal" font="default" size="100%">1094-4087</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We introduce a method for rapid determination of anisotropic terahertz absorption with sub micron resolution and high spectral integrity in the terahertz range. The method is ideal for microscopic and environmentally sensitive materials such as 2-D materials and protein crystals where the anisotropic absorption is critical to understanding underlying physics. We introduce the idea of using an iso-response relationship between the THz polarization and electro optic probe polarization to enable stationary sample polarization measurements covering a full 2 pi polarization dependence measurement. (C) 2019 Optical Society of America under the terms of the OSA Open Access Publishing Agreement&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000488282800076</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: JB0XT&lt;br/&gt;Times Cited: 1&lt;br/&gt;Cited Reference Count: 31&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Antoniou D, 2011, J PHYS CHEM B, V115, P15147, DOI 10.1021/jp207876k&lt;br/&gt;     Bagsican FR, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-01883-1&lt;br/&gt;     Baxter JB, 2006, J PHYS CHEM B, V110, P25229, DOI 10.1021/jp064399a&lt;br/&gt;     BROOKS B, 1985, P NATL ACAD SCI USA, V82, P4995, DOI 10.1073/pnas.82.15.4995&lt;br/&gt;     Chen JY, 2007, APPL PHYS LETT, V90, DOI 10.1063/1.2748852&lt;br/&gt;     Chhowalla M, 2013, NAT CHEM, V5, P263, DOI [10.1038/NCHEM.1589, 10.1038/nchem.1589]&lt;br/&gt;     Cote Y, 2017, BIOPHYS J, V112, P2575, DOI 10.1016/j.bpj.2017.05.018&lt;br/&gt;     Dhillon SS, 2017, J PHYS D APPL PHYS, V50, DOI 10.1088/1361-6463/50/4/043001&lt;br/&gt;     Docherty CJ, 2014, ACS NANO, V8, P11147, DOI 10.1021/nn5034746&lt;br/&gt;     Ebbinghaus S, 2007, P NATL ACAD SCI USA, V104, P20749, DOI 10.1073/pnas.0709207104&lt;br/&gt;     Fan ST, 2014, J PHYS D APPL PHYS, V47, DOI 10.1088/0022-3727/47/37/374009&lt;br/&gt;     George DK, 2012, J OPT SOC AM B, V29, P1406, DOI 10.1364/JOSAB.29.001406&lt;br/&gt;     GRISCHKOWSKY D, 1990, J OPT SOC AM B, V7, P2006, DOI 10.1364/JOSAB.7.002006&lt;br/&gt;     Hayes D, 2011, FARADAY DISCUSS, V150, P459, DOI 10.1039/c0fd00030b&lt;br/&gt;     Hirota Y, 2006, OPT EXPRESS, V14, P4486, DOI 10.1364/OE.14.004486&lt;br/&gt;     Huang B, 2017, NATURE, V546, P270, DOI 10.1038/nature22391&lt;br/&gt;     Jin WC, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-07547-6&lt;br/&gt;     Lang D, 2018, REV SCI INSTRUM, V89, DOI 10.1063/1.5016281&lt;br/&gt;     Markelz A, 2002, PHYS MED BIOL, V47, P3797, DOI 10.1088/0031-9155/47/21/318&lt;br/&gt;     Meireles L, 2011, PROTEIN SCI, V20, P1645, DOI 10.1002/pro.711&lt;br/&gt;     Niessen KA, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08926-3&lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;     Niessen Katherine A, 2015, Biophys Rev, V7, P201, DOI 10.1007/s12551-015-0168-4&lt;br/&gt;     Ostroverkhova O, 2006, APPL PHYS LETT, V89, DOI 10.1063/1.2387135&lt;br/&gt;     Planken PCM, 2011, J INFRARED MILLIM TE, V32, P975, DOI 10.1007/s10762-011-9824-3&lt;br/&gt;     Planken PCM, 2001, J OPT SOC AM B, V18, P313, DOI 10.1364/JOSAB.18.000313&lt;br/&gt;     Serita K, 2019, PHOTONICS-BASEL, V6, DOI 10.3390/photonics6010012&lt;br/&gt;     Vinh NQ, 2011, J AM CHEM SOC, V133, P8942, DOI 10.1021/ja200566u&lt;br/&gt;     You JW, 2018, NANO CONVERG, V5, DOI 10.1186/s40580-018-0158-x&lt;br/&gt;     Zhao C, 2017, NAT NANOTECHNOL, V12, P757, DOI [10.1038/NNANO.2017.68, 10.1038/nnano.2017.68]&lt;br/&gt;Niessen, Katherine Deng, Yanting Markelz, A. G.&lt;br/&gt;National Science FoundationNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; U.S. Department of EnergyUnited States Department of Energy (DOE) [DE-SCO016317]; National Institute of General Medical SciencesUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [STTR R41 GM125486]&lt;br/&gt;National Science Foundation (DBI 1556359, MCB 1616529); U.S. Department of Energy DE-SCO016317); National Institute of General Medical Sciences (STTR R41 GM125486).&lt;br/&gt;1&lt;br/&gt;3&lt;br/&gt;9&lt;br/&gt;Optical soc amer&lt;br/&gt;Washington</style></notes><auth-address><style face="normal" font="default" size="100%">[Niessen, Katherine|Deng, Yanting|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Markelz, AG (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;amarkelz@buffatlo.edu</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Romo, T.</style></author><author><style face="normal" font="default" size="100%">Grossfield, A.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protein Intramolecular Motions with Deuteration and Inhibitor Binding Dependence</style></title><secondary-title><style face="normal" font="default" size="100%">APS R63.003</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">03/2019</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://meetings.aps.org/Meeting/MAR19/Session/R63.3</style></url></web-urls></urls><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Romo, T.</style></author><author><style face="normal" font="default" size="100%">Grossfield, A.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Spectral Assignment of Lysozyme Collective Vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">116</style></volume><pages><style face="normal" font="default" size="100%">564A-564A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;div class=&quot;section-paragraph&quot;&gt;Global structural vibrations at terahertz (THz) frequencies have been associated with protein function and allosteric control. A chief obstacle to utilizing this control mechanism has been measurement of specific motions. Recently it was shown that while the vibrational density of states, and isotropic absorption spectra are broad and featureless, collective vibrations can be isolated based on their directionality using aligned samples (realized with protein crystals) and anisotropic THz microscopy [1]. However the assignment of resonant bands to specific structural motions was complicated by the high symmetry of the tetragonal crystals used, and the slow experimental method. To structurally map the vibrations of the chicken egg white lysozyme (CEWL) we measure anisotropic absorption of triclinic crystals using our new technique: ideal polarization varying anisotropic THz microscopy (IPV-ATM). The low symmetry triclinic crystals provide absolute protein orientation, and the near field IPV-ATM rapidly measures broadband terahertz linear dichroism of the microcrystals. All measurements were performed at room temperature under 100% humidity conditions. The unit cell parameters of triclinic lysozyme nitrate crystals, α = 28.5A°, b = 32.7A°, c = 35.1A°, α = 88.2°, β = 108.9°, γ = 111.9°, belonging to the P1 space group, were determined by X-ray diffraction before and after THz measurements. The intramolecular vibrational absorbance of the triclinic crystals has a more complex polarization dependence than the higher symmetry tetragonal crystals, as expected. While the tetragonal crystals have two strong bands at 45cm&lt;sup&gt;−1&lt;/sup&gt; and 55cm&lt;sup&gt;−1&lt;/sup&gt;, the triclinic crystals have a series of narrow bands between 40 and 60cm&lt;sup&gt;−1&lt;/sup&gt; and a prominent band at 30cm&lt;sup&gt;−1&lt;/sup&gt;. We compare the measured spectra to normal mode ensemble averaged calculations to assign the observed resonances, and isolating which collective motions impact the catalytic site.&lt;/div&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000460779802832</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 1&lt;br/&gt;Cited References: &lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;Deng, Yanting Mckinney, Jeffrey Romo, Tod Grossfield, Alan Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Mckinney, Jeffrey|Markelz, Andrea] SUNY Buffalo, Phys, Buffalo, NY USA. [Romo, Tod|Grossfield, Alan] Univ Rochester, Med Ctr, Dept Biochem &amp; Biophys, Rochester, NY 14642 USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Luck, C. H.</style></author><author><style face="normal" font="default" size="100%">Romo, T. D.</style></author><author><style face="normal" font="default" size="100%">Grossfield, A. M.</style></author><author><style face="normal" font="default" size="100%">Bandara, S.</style></author><author><style face="normal" font="default" size="100%">Ren, Z.</style></author><author><style face="normal" font="default" size="100%">Yang, X. J.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Increase in Dynamical Collectivity and Directionality of Orange Carotenoid Protein in the Photo-Protective State</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">114</style></volume><pages><style face="normal" font="default" size="100%">522A-522A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000430563200362</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: GD5RB&lt;br/&gt;Times Cited: 1&lt;br/&gt;Cited Reference Count: 0&lt;br/&gt;Deng, Yanting Luck, Catherine H. Romo, Tod D. Grossfield, Alan M. Bandara, Sepalika Ren, Zhong Yang, Xiaojing Markelz, Andrea G.&lt;br/&gt;62nd Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 17-21, 2018&lt;br/&gt;San Francisco, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;1&lt;br/&gt;&lt;br/&gt;7&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Luck, Catherine H.|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Romo, Tod D.|Grossfield, Alan M.] Univ Rochester, Med Ctr, Dept Biochem &amp; Biophys, Rochester, NY 14642 USA. 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B.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The 2017 terahertz science and technology roadmap</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Physics D-Applied Physics</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Phys. D-Appl. Phys.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">ex-vivo</style></keyword><keyword><style  face="normal" font="default" size="100%">generation</style></keyword><keyword><style  face="normal" font="default" size="100%">metal wave-guides</style></keyword><keyword><style  face="normal" font="default" size="100%">near-field</style></keyword><keyword><style  face="normal" font="default" size="100%">performance</style></keyword><keyword><style  face="normal" font="default" size="100%">photoconductive emitters</style></keyword><keyword><style  face="normal" font="default" size="100%">Physics</style></keyword><keyword><style  face="normal" font="default" size="100%">quantum-cascade lasers</style></keyword><keyword><style  face="normal" font="default" size="100%">radiation</style></keyword><keyword><style  face="normal" font="default" size="100%">semiconductors</style></keyword><keyword><style  face="normal" font="default" size="100%">Terahertz</style></keyword><keyword><style  face="normal" font="default" size="100%">thz</style></keyword><keyword><style  face="normal" font="default" size="100%">time-domain spectroscopy</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><volume><style face="normal" font="default" size="100%">50</style></volume><pages><style face="normal" font="default" size="100%">49</style></pages><isbn><style face="normal" font="default" size="100%">0022-3727</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Science and technologies based on terahertz frequency electromagnetic radiation (100 GHz-30 THz) have developed rapidly over the last 30 years. For most of the 20th Century, terahertz radiation, then referred to as sub-millimeter wave or far-infrared radiation, was mainly utilized by astronomers and some spectroscopists. Following the development of laser based terahertz time-domain spectroscopy in the 1980s and 1990s the field of THz science and technology expanded rapidly, to the extent that it now touches many areas from fundamental science to &#039;real world&#039; applications. For example THz radiation is being used to optimize materials for new solar cells, and may also be a key technology for the next generation of airport security scanners. While the field was emerging it was possible to keep track of all new developments, however now the field has grown so much that it is increasingly difficult to follow the diverse range of new discoveries and applications that are appearing. At this point in time, when the field of THz science and technology is moving from an emerging to a more established and interdisciplinary field, it is apt to present a roadmap to help identify the breadth and future directions of the field. The aim of this roadmap is to present a snapshot of the present state of THz science and technology in 2017, and provide an opinion on the challenges and opportunities that the future holds. To be able to achieve this aim, we have invited a group of international experts to write 18 sections that cover most of the key areas of THz science and technology. We hope that The 2017 Roadmap on THz science and technology will prove to be a useful resource by providing a wide ranging introduction to the capabilities of THz radiation for those outside or just entering the field as well as providing perspective and breadth for those who are well established. 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S. Vitiello, M. S. Linfield, E. H. Davies, A. G. Hoffmann, Matthias C. Booske, John Paoloni, Claudio Gensch, M. Weightman, P. Williams, G. P. Castro-Camus, E. Cumming, D. R. S. Simoens, F. Escorcia-Carranza, I. Grant, J. Lucyszyn, Stepan Kuwata-Gonokami, Makoto Konishi, Kuniaki Koch, Martin Schmuttenmaer, Charles A. Cocker, Tyler L. Huber, Rupert Markelz, A. G. Taylor, Z. D. Wallace, Vincent P. Zeitler, J. Axel Sibik, Juraj Korter, Timothy M. Ellison, B. Rea, S. Goldsmith, P. Cooper, Ken B. Appleby, Roger Pardo, D. Huggard, P. G. Krozer, V. Shams, Haymen Fice, Martyn Renaud, Cyril Seeds, Alwyn Stoehr, Andreas Naftaly, Mira Ridler, Nick Clarke, Roland Cunningham, John E. Johnston, Michael B.&lt;br/&gt;Huggard, Peter/U-2150-2019; Konishi, Kuniaki/AAN-3624-2020; Zeitler, J. Axel/B-4885-2008; Paoloni, Claudio/AAH-9824-2019; Hoffmann, Matthias C./N-1082-2019; Wallace, Vincent P/A-9320-2012; Johnston, Michael/B-9813-2008; Castro-Camus, Enrique/V-6861-2019; Krozer, Viktor/P-5623-2014; Hoffmann, Matthias C/B-3893-2009; PAOLONI, CLAUDIO/AAA-3211-2020; Gonokami, Makoto/F-3641-2012; Shams, Haymen/H-3754-2012; Ridler, Nick/AAN-9637-2020; Huber, Rupert/N-4126-2018&lt;br/&gt;Konishi, Kuniaki/0000-0003-2389-9787; Zeitler, J. Axel/0000-0002-4958-0582; Hoffmann, Matthias C./0000-0002-3596-9853; Wallace, Vincent P/0000-0003-3814-5400; Johnston, Michael/0000-0002-0301-8033; Krozer, Viktor/0000-0002-2387-1947; Hoffmann, Matthias C/0000-0002-3596-9853; PAOLONI, CLAUDIO/0000-0002-0265-0862; Shams, Haymen/0000-0002-5333-6478; Huber, Rupert/0000-0001-6617-9283; Davies, Alexander/0000-0002-1987-4846; Seeds, Alwyn/0000-0002-5228-627X; Castro-Camus, Enrique/0000-0002-8218-9155; Cunningham, John/0000-0002-1805-9743; Naftaly, Mira/0000-0002-0671-822X; Cumming, David/0000-0002-7838-8362&lt;br/&gt;Engineering and Physical Sciences Research CouncilUK Research &amp; Innovation (UKRI)Engineering &amp; Physical Sciences Research Council (EPSRC) [EP/P015883/1, EP/M00306X/1, EP/K023349/1, EP/M017095/1, EP/L026597/1, EP/J017671/1] Funding Source: researchfish; Natural Environment Research CouncilUK Research &amp; Innovation (UKRI)NERC Natural Environment Research Council [NER/Z/S/2003/00642, NE/L012375/1, NER/Z/S/2000/01292] Funding Source: researchfish; Science and Technology Facilities CouncilUK Research &amp; Innovation (UKRI)Science &amp; Technology Facilities Council (STFC) [ST/P002056/1] Funding Source: researchfish; Direct For Biological SciencesNational Science Foundation (NSF)NSF - Directorate for Biological Sciences (BIO) [1556359] Funding Source: National Science Foundation; Div Of Biological InfrastructureNational Science Foundation (NSF)NSF - Directorate for Biological Sciences (BIO) [1556359] Funding Source: National Science Foundation; Div Of Molecular and Cellular BioscienceNational Science Foundation (NSF)NSF - Directorate for Biological Sciences (BIO) [1616529] Funding Source: National Science Foundation&lt;br/&gt;566&lt;br/&gt;30&lt;br/&gt;462&lt;br/&gt;Iop publishing ltd&lt;br/&gt;Bristol&lt;br/&gt;1361-6463</style></notes><custom7><style face="normal" font="default" size="100%">043001</style></custom7><auth-address><style face="normal" font="default" size="100%">[Dhillon, S. S.] Univ Paris 06, Univ Paris Diderot, Sorbonne Univ,CNRS,Lab Pierre Aigrain, Sorbonne Paris Cite,Ecole Normale Super,PSL Res U, F-75231 Paris, France. [Vitiello, M. S.] CNR, Ist Nanosci, NEST, Piazza San Silvestro 12, I-56127 Pisa, Italy. [Vitiello, M. S.] Scuola Normale Super Pisa, Piazza San Silvestro 12, I-56127 Pisa, Italy. [Linfield, E. H.|Davies, A. G.|Cunningham, John E.] Univ Leeds, Sch Elect &amp; Elect Engn, Leeds LS2 9JT, W Yorkshire, England. [Hoffmann, Matthias C.] SLAC Natl Accelerator Lab, Linac Coherent Light Source, Menlo Pk, CA 94025 USA. [Booske, John] Univ Wisconsin Madison, Dept Elect &amp; Comp Engn, Madison, WI USA. [Paoloni, Claudio] Univ Lancaster, Dept Engn, Lancaster, England. [Gensch, M.] Helmholtz Zentrum Dresden Rossendorf, Inst Radiat Phys, Bautzner Landstr 400, D-01328 Dresden, Germany. [Weightman, P.] Univ Liverpool, Dept Phys, Liverpool L69 7ZE, Merseyside, England. [Williams, G. P.] Jefferson Lab, 12000 Jefferson Ave Suite 21, Newport News, VA 23606 USA. [Castro-Camus, E.] Ctr Invest Opt AC, Loma Bosque 115, Guanajuato 37150, Mexico. [Cumming, D. R. S.|Escorcia-Carranza, I.|Grant, J.] Glasgow, Sch Engn, Microsyst Technol Grp, Glasgow G12 8LT, Lanark, Scotland. [Simoens, F.] CEA Leti MINATEC, 17 Rue Martyrs, F-38054 Grenoble 9, France. [Lucyszyn, Stepan] Imperial Coll London, Dept EEE, Ctr Terahertz Sci &amp; Engn, London, England. [Kuwata-Gonokami, Makoto|Konishi, Kuniaki] Univ Tokyo, Dept Phys, Tokyo, Japan. [Koch, Martin] Philipps Univ Marburg, Fac Phys, D-35032 Marburg, Germany. [Koch, Martin] Philipps Univ Marburg, Ctr Mat Sci, D-35032 Marburg, Germany. [Schmuttenmaer, Charles A.] Yale Univ, Dept Chem, 225 Prospect St,POB 208107, New Haven, CT 06520 USA. [Schmuttenmaer, Charles A.] Yale Univ, Energy Sci Inst, 225 Prospect St,POB 208107, New Haven, CT 06520 USA. [Cocker, Tyler L.|Huber, Rupert] Univ Regensburg, Inst Expt &amp; Angew Phys, Univ Str 31, D-93053 Regensburg, Germany. [Markelz, A. G.] Univ Buffalo State Univ New York, Dept Phys, Buffalo, NY 14620 USA. [Taylor, Z. D.] Univ Calif Los Angeles, Dept Bioengn, Los Angeles, CA 90095 USA. [Wallace, Vincent P.] Univ Western Australia M013, 35 Stirling Highway, Crawley, WA 6009, Australia. [Zeitler, J. Axel|Sibik, Juraj] Magnet Resonance Res Ctr, Dept Chem Engn, JJ Thompson Ave, Cambridge CB3 0HE, England. [Korter, Timothy M.] Syracuse Univ, Dept Chem, 1-014 CST,111 Coll Pl, Syracuse, NY 13244 USA. [Ellison, B.|Rea, S.|Pardo, D.|Huggard, P. G.] RAL Space, STFC, Millimetre Wave Technol Grp, Didcot OX11 0QX, Oxon, England. [Goldsmith, P.] Jet Prop Lab, M-S 180-703,4800 Oak Grove Dr, Pasadena, CA 91109 USA. [Cooper, Ken B.] CALTECH, Jet Prop Lab, Pasadena, CA USA. [Appleby, Roger] Innovasec Ltd, 212b West Malvern Rd, Malvern WR14 4BA, Worcs, England. [Krozer, V.] Goethe Univ Frankfurt Main, Goethe Leibniz Terahertz Ctr, D-60323 Frankfurt, Germany. [Shams, Haymen|Fice, Martyn|Renaud, Cyril|Seeds, Alwyn] UCL, Dept Elect &amp; Elect Engn, Torrington Pl, London WC1E 7JE, England. [Stoehr, Andreas] Univ Duisburg Essen, Fac Engn, Dept Optoelect, Lotharstr 55, D-47057 Duisburg, Germany. [Naftaly, Mira|Ridler, Nick] Natl Phys Lab, Div Time Quantum &amp; Electromagnet, Teddington TW11 0LW, Middx, England. [Clarke, Roland] Univ Leeds, Sch Elect &amp; Elect Engn, Leeds LS2 9JT, W Yorkshire, England. [Johnston, Michael B.] Univ Oxford, Dept Phys, Clarendon Lab, Parks Rd, Oxford OX1 3PU, England.&lt;br/&gt;Cunningham, JE (corresponding author), Univ Leeds, Sch Elect &amp; Elect Engn, Leeds LS2 9JT, W Yorkshire, England.|Johnston, MB (corresponding author), Univ Oxford, Dept Phys, Clarendon Lab, Parks Rd, Oxford OX1 3PU, England.&lt;br/&gt;enrique@cio.mx|david.cumming.2@glasgow.ac.uk|J.E.Cunningham@leeds.ac.uk|michael.johnston@physics.ox.ac.uk</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Xu, M. Y.</style></author><author><style face="normal" font="default" size="100%">Niessen, K. A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Michki, N. S.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Escaping the Water Cage: Protein Intramolecular Vibrations and the Dynamical Transition</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">112</style></volume><pages><style face="normal" font="default" size="100%">318A-318A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000402375600574</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: EW3DR&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 0&lt;br/&gt;Xu, Mengyang Niessen, Katherine A. Deng, Yanting Michki, Nigel S. Markelz, Andrea G.&lt;br/&gt;58th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2014&lt;br/&gt;San Francisco, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;NSFNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; DOEUnited States Department of Energy (DOE) [DE-SC0016317]&lt;br/&gt;This work was supported by NSF (DBI 1556359 and MCB 1616529), and DOE DE-SC0016317.&lt;br/&gt;&lt;br/&gt;7&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Xu, Mengyang|Niessen, Katherine A.|Deng, Yanting|Michki, Nigel S.|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">Xu, M.</style></author><author><style face="normal" font="default" size="100%">Liu, H.</style></author><author><style face="normal" font="default" size="100%">Blankenship, R.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Global Picosecond Structural Dynamics of Orange Carotenoid Protein in Photo/Chemical Activated Signaling States</style></title><secondary-title><style face="normal" font="default" size="100%">APS 2017 S4.002</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">03/2017</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://meetings.aps.org/link/BAPS.2017.MAR.S4.2</style></url></web-urls></urls><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Niessen, Katherine A.</style></author><author><style face="normal" font="default" size="100%">Xu, Mengyang</style></author><author><style face="normal" font="default" size="100%">Deng, Yanting</style></author><author><style face="normal" font="default" size="100%">Snell, Edward H.</style></author><author><style face="normal" font="default" size="100%">Markelz, Andrea G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Importance of Protein Vibration Directionality on Function</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb 3</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">112</style></volume><pages><style face="normal" font="default" size="100%">353A-353A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><accession-num><style face="normal" font="default" size="100%">WOS:000402375600746</style></accession-num><notes><style face="normal" font="default" size="100%">Snell, Edward/G-2055-2018&lt;br/&gt;Snell, Edward/0000-0001-8714-3191&lt;br/&gt;1&lt;br/&gt;58th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2014&lt;br/&gt;San Francisco, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;</style></notes></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Xu, M. Y.</style></author><author><style face="normal" font="default" size="100%">Liu, H. J.</style></author><author><style face="normal" font="default" size="100%">Blankenship, R. E.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Orange Carotenoid Protein Picosecond Dynamics Changes with Photo and Chemical Activation</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">112</style></volume><pages><style face="normal" font="default" size="100%">441A-441A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000402375700177</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: EW3DS&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 3&lt;br/&gt;Cited References: &lt;br/&gt;     King JD, 2014, FEBS LETT, V588, P4561, DOI 10.1016/j.febslet.2014.10.024&lt;br/&gt;     Wilson A, 2006, PLANT CELL, V18, P992, DOI 10.1105/tpc.105.040121&lt;br/&gt;     Wilson A, 2008, P NATL ACAD SCI USA, V105, P12075, DOI 10.1073/pnas.0804636105&lt;br/&gt;Deng, Yanting Xu, Mengyang Liu, Haijun Blankenship, Robert E. Markelz, Andrea G.&lt;br/&gt;58th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2014&lt;br/&gt;San Francisco, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;Liu, Haijun/0000-0003-0537-0302&lt;br/&gt;&lt;br/&gt;14&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Xu, Mengyang|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Liu, Haijun|Blankenship, Robert E.] Washington Univ, Dept Biol, Campus Box 1137, St Louis, MO 63130 USA. [Liu, Haijun|Blankenship, Robert E.] Washington Univ, Dept Chem, St Louis, MO 63130 USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>10</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Xu, M. Y.</style></author><author><style face="normal" font="default" size="100%">Niessen, K.</style></author><author><style face="normal" font="default" size="100%">Michki, N.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Snell, E.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Anisotropic Absorption Measurements Reveal Protein Dynamical Transition in Intramolecular Vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">2016 41st International Conference on Infrared, Millimeter, and Terahertz Waves</style></secondary-title><tertiary-title><style face="normal" font="default" size="100%">International Conference on Infrared Millimeter and Terahertz Waves</style></tertiary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year></dates><publisher><style face="normal" font="default" size="100%">Ieee</style></publisher><pub-location><style face="normal" font="default" size="100%">New York</style></pub-location><isbn><style face="normal" font="default" size="100%">978-1-4673-8485-8</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Modeling has predicted that intramolecular structural vibrations enables proteins to access functionally important structural change. We show that the vibrational density of states and the isotropic absorption in the terahertz range are only weakly dependent on the protein functional state for several bench marking proteins. At the same time the direction of motions changes dramatically with functional state and with a resulting impact on the anisotropic absorption. Our anisotropic THz microscopy (ATM) measurements confirm this sensitivity. Here we apply the technique to the question of whether the protein dynamical transition (DT) is important to protein function. We find a strong anisotropic resonance at 70 cm(-1) rapidly increases in strength at temperatures above the DT. As these intramolecular vibrations enable protein structure to change conformation, the results suggest function will cease below DT for those proteins that require large scale conformational change.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000391406200009</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BG7KC&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 4&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Niessen K., 2015, BIOPHYSICAL REV&lt;br/&gt;     PETHIG R, 1995, PROTEIN SOLVENT INTE, P265&lt;br/&gt;     RUPLEY JA, 1991, ADV PROTEIN CHEM, V41, P37&lt;br/&gt;Xu, Mengyang Niessen, Katherine Michki, Nigel Deng, Yanting Snell, Edward Markelz, A. G.&lt;br/&gt;Irmmw-thz&lt;br/&gt;Proceedings Paper&lt;br/&gt;41st International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)&lt;br/&gt;Sep 25-30, 2016&lt;br/&gt;Copenhagen, DENMARK&lt;br/&gt;DTU, IEEE, QMC Instruments, Danish Ctr Laser Infrastructure, DTU Fotonik, Dept Photon Engn, ARL, Carl Sberg Fdn, AF Off Sci Res, Tech Univ Denmark, IEEE Microwave Theory &amp; Tech Soc, Azpect Photon, Ekspla, Hubner HF Syst Engn, I2S, Laser Quantum, Menlo Syst, Neaspec, Springer, TeraView, Virginia Diodes&lt;br/&gt;Snell, Edward/G-2055-2018&lt;br/&gt;Snell, Edward/0000-0001-8714-3191&lt;br/&gt;345 e 47th st, new york, ny 10017 usa&lt;br/&gt;2162-2027</style></notes><auth-address><style face="normal" font="default" size="100%">[Xu, Mengyang|Niessen, Katherine|Michki, Nigel|Deng, Yanting|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Snell, Edward] Hauptman Woodward Med Res Inst, Buffalo, NY USA.&lt;br/&gt;Xu, MY (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Yanting</style></author><author><style face="normal" font="default" size="100%">Xu, Mengyang</style></author><author><style face="normal" font="default" size="100%">Niessen, Katherine A.</style></author><author><style face="normal" font="default" size="100%">Schmidt, Marius</style></author><author><style face="normal" font="default" size="100%">Markelz, Andrea G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Direct Measurements of the Long-Range Collective Vibrations of Photoactive Yellow Protein</style></title><secondary-title><style face="normal" font="default" size="100%">30th Anniversary Symposium of The Protein Society</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://onlinelibrary.wiley.com/doi/10.1002/pro.3026</style></url></web-urls></urls><pub-location><style face="normal" font="default" size="100%">Baltimore MD</style></pub-location><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;Long-range collective vibrations are thought to be crucial to protein functions. In the case of photoactive protein family, modeling suggests the intramolecular vibrations provide an efficient means of energy relaxation[1], feedback for enhancement of chromophore vibrations that promote structural transitions[2] and can assist in charge energy transfer[3]. As a paradigm of this family, photoactive yellow protein (PYP) is a cytoplasmic photocycling protein related to negative phototactic response to blue light in purple photosynthetic bacteria. PYP has a p-coumaric acid chromophore binding to the cysteine residue via a thioester bond, whose vibrations were found to overlap calculated vibrations of the protein scaffold. Using our unique technique of anisotropic terahertz microscopy(ATM)[4], we measure the intramolecular vibrations for PYP for the first time, including cycling between ground and blue shift (pB) states. Room temperature ATM measurements are performed in the dark and with continuous wave illumination at 488nm, resulting in a steady pB state with approximately 5% population conversion. In pB state, we find an overall decrease in the strength of resonant band in frequency range of 30-60 cm-1. Our calculated spectra using quasi-harmonic analysis indicate that our measurements are dominated by the protein vibrations, rather than the pCA chromophore, allowing us to characterize how the scaffold dynamics changes with functional states and mutations.&lt;/p&gt;

&lt;p&gt;1. Levantino, M., et al. Nat Commun, 2015. 6.&lt;/p&gt;

&lt;p&gt;2. Mataga, N., et al. Chem. Phys. Lett., 2002. 352(3-4): p. 220-225.&lt;/p&gt;

&lt;p&gt;3. Fokas, A.S., et al. Photosynth. Res., 2014. 122&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Xu, Mengyang</style></author><author><style face="normal" font="default" size="100%">Niessen, Katherine</style></author><author><style face="normal" font="default" size="100%">Deng, Yanting</style></author><author><style face="normal" font="default" size="100%">Michki, Nigel</style></author><author><style face="normal" font="default" size="100%">Snell, Edward</style></author><author><style face="normal" font="default" size="100%">Markelz, Andrea</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%"> The Role of Dynamical Transition in Protein Function: Coupling of Protein Collective Vibrations and Water Dynamics</style></title><secondary-title><style face="normal" font="default" size="100%">30th Anniversary Symposium of The Protein Society</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://onlinelibrary.wiley.com/doi/10.1002/pro.3026</style></url></web-urls></urls><pub-location><style face="normal" font="default" size="100%">Baltimore, MD</style></pub-location><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;Computational simulations have revealed protein collective vibrations prompt structural rearrangements to accomplish biological function. However, the biological importance of collective vibrations has not been experimentally demonstrated. The attempts have been hampered by the inability to distinguish localized water or side-chain relaxational motions from protein long-range vibrations using conventional techniques. The dynamical transition (DT), extensively observed using X-ray, neutron scattering, NMR and terahertz techniques [1,2], describes a rapid increase in the temperature-dependent dynamics of critically hydrated proteins above ∼220 K, and has been attributed to thermally activated solvent motions. While some proteins lose function below the specific temperature, others do not. We suggest the difference arises from the nature of the required motions for function. Specifically, functional motions enabled by long-range vibrations will be vulnerable to DT, which require surrounding solvent to be sufficiently mobile. We explored the coupling of protein vibrations to solvent dynamics by applying a recently developed technique, anisotropy terahertz microscopy [3], to directly measure the collective vibrations for lysozyme and investigate the temperature dependence in 150-300 K range. We find long-range intramolecular vibrations occur at 220K and rapidly increase in strength with increasing temperature, consistent with enhanced access above the DT. The results suggest collective vibrations are slaved to DT, and those proteins with function reliant on these motions will cease function below DT.&lt;/p&gt;

&lt;p&gt;1. Doster,W., et al. Phys.Rev.Lett., 2010.104(9):098101.&lt;/p&gt;

&lt;p&gt;2. Niessen,K., et al. Biophys.Rev., 2015.7,201.&lt;/p&gt;

&lt;p&gt;3. Acbas,G., et al. Nat.Commun., 2014.5,3076.&lt;/p&gt;
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