<?xml version="1.0" encoding="UTF-8"?><xml><records><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%">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>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Singh, R.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Bae, C. J.</style></author><author><style face="normal" font="default" size="100%">Niessen, K. 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%">Modulated orientation-sensitive terahertz spectroscopy</style></title><secondary-title><style face="normal" font="default" size="100%">Photonics Research</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Photonics Res.</style></alt-title><short-title><style face="normal" font="default" size="100%">Photonics Res.Photonics Res.</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">absorption-spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">enzyme catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">low-frequency modes</style></keyword><keyword><style  face="normal" font="default" size="100%">lysozyme</style></keyword><keyword><style  face="normal" font="default" size="100%">neutron-scattering</style></keyword><keyword><style  face="normal" font="default" size="100%">Optics</style></keyword><keyword><style  face="normal" font="default" size="100%">perspective</style></keyword><keyword><style  face="normal" font="default" size="100%">polarization modulation</style></keyword><keyword><style  face="normal" font="default" size="100%">proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">water</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Jun</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">A1-A8</style></pages><isbn><style face="normal" font="default" size="100%">2327-9125</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Intramolecular vibrations of large macromolecules reside in the terahertz range. In particular, protein vibrations are closely spaced in frequency, resulting in a nearly continuous vibrational density of states. This density of vibrations interferes with the identification of specific absorption lines and their subsequent association with specific functional motions. This challenge is compounded with the absorption being dominated by the solvent and local relaxational motions. A strategy for removing the isotropic relaxational loss and isolating specific vibrations is to use aligned samples and polarization-sensitive measurements. Here, we demonstrate a technique to rapidly attain the anisotropic resonant absorbance using terahertz time domain spectroscopy and a spinning sample. The technique, modulated orientation-sensitive terahertz spectroscopy (MOSTS), has a nonzero signal only for anisotropic samples, as demonstrated by a comparison between a silicon wafer and a wire grid polarizer. For sucrose and oxalic acid molecular crystals, the MOSTS response is in agreement with modeled results for the intermolecular vibrations. Further, we demonstrate that, even in the presence of a large relaxational background, MOSTS isolates underlying vibrational resonances. (C) 2016 Chinese Laser Press&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:000376658500001</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: DM9BJ&lt;br/&gt;Times Cited: 6&lt;br/&gt;Cited Reference Count: 40&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Aguilar RV, 2012, PHYS REV LETT, V108, DOI 10.1103/PhysRevLett.108.087403&lt;br/&gt;     Aschaffenburg DJ, 2012, APPL PHYS LETT, V100, DOI 10.1063/1.4729148&lt;br/&gt;     Bahar I, 2005, CURR OPIN STRUC BIOL, V15, P586, DOI 10.1016/j.sbi.2005.08.007&lt;br/&gt;     Benkovic SJ, 2003, SCIENCE, V301, P1196, DOI 10.1126/science.1085515&lt;br/&gt;     Boehr DD, 2006, CHEM REV, V106, P3055, DOI 10.1021/cr050312q&lt;br/&gt;     Chen JY, 2005, PHYS REV E, V72, DOI 10.1103/PhysRevE.72.040901&lt;br/&gt;     Chen Q, 1999, APPL PHYS LETT, V74, P3435, DOI 10.1063/1.124119&lt;br/&gt;     Daniel RM, 2003, ANNU REV BIOPH BIOM, V32, P69, DOI 10.1146/annurev.biophys.32.110601.142445&lt;br/&gt;     Diehl M, 1997, BIOPHYS J, V73, P2726, DOI 10.1016/S0006-3495(97)78301-2&lt;br/&gt;     Ebbinghaus S, 2007, P NATL ACAD SCI USA, V104, P20749, DOI 10.1073/pnas.0709207104&lt;br/&gt;     Falconer RJ, 2012, J INFRARED MILLIM TE, V33, P973, DOI 10.1007/s10762-012-9915-9&lt;br/&gt;     Fan ST, 2014, J PHYS D APPL PHYS, V47, DOI 10.1088/0022-3727/47/37/374009&lt;br/&gt;     Frauenfelder H, 2006, P NATL ACAD SCI USA, V103, P15469, DOI 10.1073/pnas.0607168103&lt;br/&gt;     Gabel F, 2002, Q REV BIOPHYS, V35, P327, DOI 10.1017/S0033583502003840&lt;br/&gt;     George DK, 2012, J OPT SOC AM B, V29, P1406, DOI 10.1364/JOSAB.29.001406&lt;br/&gt;     Giraud G, 2003, BIOPHYS J, V85, P1903, DOI 10.1016/S0006-3495(03)74618-9&lt;br/&gt;     Hammes GG, 2011, BIOCHEMISTRY-US, V50, P10422, DOI 10.1021/bi201486f&lt;br/&gt;     Jackson J.D., 1975, CLASSICAL ELECTRODYN&lt;br/&gt;     Jenkins GS, 2010, REV SCI INSTRUM, V81, DOI 10.1063/1.3480554&lt;br/&gt;     Jepsen PU, 2007, CHEM PHYS LETT, V442, P275, DOI 10.1016/j.cplett.2007.05.112&lt;br/&gt;     Karplus M, 2005, P NATL ACAD SCI USA, V102, P6679, DOI 10.1073/pnas.0408930102&lt;br/&gt;     Kim SJ, 2008, ANGEW CHEM INT EDIT, V47, P6486, DOI 10.1002/anie.200802281&lt;br/&gt;     Kindt JT, 1996, J PHYS CHEM-US, V100, P10373, DOI 10.1021/jp960141g&lt;br/&gt;     King MD, 2010, J PHYS CHEM A, V114, P7127, DOI 10.1021/jp101935n&lt;br/&gt;     Kroll J, 2007, VIB SPECTROSC, V43, P324, DOI 10.1016/j.vibspec.2006.03.010&lt;br/&gt;     Leitner DM, 2008, HFSP J, V2, P314, DOI 10.2976/1.2976661&lt;br/&gt;     Li M, 2011, OPT LETT, V36, P3633, DOI 10.1364/OL.36.003633&lt;br/&gt;     Liu D, 2008, PHYS REV LETT, V101, DOI 10.1103/PhysRevLett.101.135501&lt;br/&gt;     Niessen Katherine A, 2015, Biophys Rev, V7, P201, DOI 10.1007/s12551-015-0168-4&lt;br/&gt;     PETHIG R, 1995, PROTEIN SOLVENT INTE, P265&lt;br/&gt;     Planken PCM, 2001, J OPT SOC AM B, V18, P313, DOI 10.1364/JOSAB.18.000313&lt;br/&gt;     Rheinstadter MC, 2009, PHYS REV LETT, V103, DOI 10.1103/PhysRevLett.103.128104&lt;br/&gt;     RUPLEY JA, 1991, ADV PROTEIN CHEM, V41, P37&lt;br/&gt;     Singh R, 2012, J PHYS CHEM A, V116, P10359, DOI 10.1021/jp307288r&lt;br/&gt;     TORGESEN JL, 1964, SCIENCE, V146, P53, DOI 10.1126/science.146.3640.53&lt;br/&gt;     Vinh NQ, 2011, J AM CHEM SOC, V133, P8942, DOI 10.1021/ja200566u&lt;br/&gt;     Walther M, 2003, CHEM PHYS, V288, P261, DOI 10.1016/S0301-0104(03)00031-4&lt;br/&gt;     Xu J, 2006, J PHYS CHEM B, V110, P24255, DOI 10.1021/jp064830w&lt;br/&gt;     Yasumatsu N, 2012, REV SCI INSTRUM, V83, DOI 10.1063/1.3683570&lt;br/&gt;Singh, Rohit George, Deepu Koshy Bae, Chejin Niessen, K. A. Markelz, A. G.&lt;br/&gt;George, Deepu/J-9882-2014&lt;br/&gt;George, Deepu/0000-0003-0021-0705&lt;br/&gt;National Science Foundation (NSF)National Science Foundation (NSF) [DBI2959989]; University at Buffalo (UB) [1126960-1-68255]; Los Alamos National Laboratory (LANL)United States Department of Energy (DOE)Los Alamos National Laboratory [1125895-1-71842]; 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&lt;br/&gt;National Science Foundation (NSF) (DBI2959989); University at Buffalo (UB) (Holm Fund 1126960-1-68255); Los Alamos National Laboratory (LANL) (Molecular Crystal Studies 1125895-1-71842).&lt;br/&gt;6&lt;br/&gt;&lt;br/&gt;26&lt;br/&gt;Optical soc amer&lt;br/&gt;Washington</style></notes><auth-address><style face="normal" font="default" size="100%">[Singh, Rohit] Depauw Univ, Dept Phys &amp; Astron, Greencastle, IN 46135 USA. [George, Deepu Koshy] Virginia Tech, Dept Phys, Blacksburg, VA 24061 USA. [Bae, Chejin] Univ Buffalo, Dept Elect Engn, Buffalo, NY 14260 USA. [Niessen, K. A.|Markelz, A. G.] Univ Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Markelz, AG (corresponding author), Univ Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;amarkelz@buffalo.edu</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. A.</style></author><author><style face="normal" font="default" size="100%">Xu, M.</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%">Terahertz Optical Measurements of Correlated Motions with Possible Allosteric 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%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">04/2015</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5425745/</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">201–216</style></pages><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>10</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Niessen, K. A.</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%">Measurements and Calculations of Protein Intramolecular Vibrations in the THz Range</style></title><secondary-title><style face="normal" font="default" size="100%">2014 39th 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><keywords><keyword><style  face="normal" font="default" size="100%">charmm</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</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%">978-1-4799-3877-3</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 report the calculations and measurements of intramolecular vibrational modes and their dependence on inhibitor binding in the THz range. We see an increase in anisotropic THz absorption at low frequency with inhibitor binding in both the measurements and calculations. This surprising result suggests an increase in flexibility with binding. We will discuss the possible reasons for this discrepancy.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000378889200091</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BF0IL&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 13&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Balog E, 2004, PHYS REV LETT, V93, DOI 10.1103/PhysRevLett.93.028103&lt;br/&gt;     Best RB, 2012, J CHEM THEORY COMPUT, V8, P3257, DOI 10.1021/ct300400x&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     BRUCCOLERI RE, 1986, BIOPOLYMERS, V25, P1767, DOI 10.1002/bip.360250916&lt;br/&gt;     CHEETHAM JC, 1992, J MOL BIOL, V224, P613, DOI 10.1016/0022-2836(92)90548-X&lt;br/&gt;     Dong J, 1999, ACTA CRYSTALLOGR D, V55, P745, DOI 10.1107/S0907444998016047&lt;br/&gt;     Guo JN, 2014, BIOCHEMISTRY-US, V53, P2855, DOI 10.1021/bi500238q&lt;br/&gt;     Hammes-Schiffer S, 2006, ANNU REV BIOCHEM, V75, P519, DOI 10.1146/annurev.biochem.75.103004.142800&lt;br/&gt;     Henzler-Wildman KA, 2007, NATURE, V450, P838, DOI 10.1038/nature06410&lt;br/&gt;     Jo S, 2008, J COMPUT CHEM, V29, P1859, DOI 10.1002/jcc.20945&lt;br/&gt;     PERUTZ MF, 1970, NATURE, V228, P726, DOI 10.1038/228726a0&lt;br/&gt;     TEETER MM, 1990, J PHYS CHEM-US, V94, P8091, DOI 10.1021/j100384a021&lt;br/&gt;Niessen, Katherine A. Snell, Edward Markelz, A. G.&lt;br/&gt;Irmmw-thz&lt;br/&gt;Proceedings Paper&lt;br/&gt;39th International Conference on Infrared, Millimeter, and Terahertz waves (IRMMW-THz)&lt;br/&gt;Sep 14-19, 2014&lt;br/&gt;Tucson, AZ&lt;br/&gt;THORLABS, Tydex, TOPTICA Photon, Bruker, Gentec EO, Lake Shore Cryotron, Ekspla, Zomega, TeraSense, Insight Product, Emcore, QMC Instruments, TeraView, NeaSpec, Advantest, MenloSystems, Traycer, Microtech Instruments Inc, LongWave Photon, Virginia Diodes Inc, ASU, MTT S, Journal Infrared Millimeter &amp; Tera Hertz Waves, Tera Hertz Sci &amp; Technol, Army Res Off&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%">[Niessen, Katherine A.|Markelz, A. G.] SUNY Buffalo, Univ Buffalo, Dept Phys, Buffalo, NY 14260 USA. [Snell, Edward|Markelz, A. G.] SUNY Buffalo, Univ Buffalo, Hauptman Woodward Med Res Inst, Buffalo, NY 14203 USA. [Snell, Edward|Markelz, A. G.] SUNY Buffalo, Univ Buffalo, Dept Biol Struct, Buffalo, NY 14203 USA.&lt;br/&gt;Niessen, KA (corresponding author), SUNY Buffalo, 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%">Acbas, G.</style></author><author><style face="normal" font="default" size="100%">Niessen, K. A.</style></author><author><style face="normal" font="default" size="100%">Snell, E. H.</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%">Optical measurements of long-range protein vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">Nature Communications</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Nat. Commun.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">absorption</style></keyword><keyword><style  face="normal" font="default" size="100%">crystals</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">frequency raman-spectra</style></keyword><keyword><style  face="normal" font="default" size="100%">hydration</style></keyword><keyword><style  face="normal" font="default" size="100%">lysozyme</style></keyword><keyword><style  face="normal" font="default" size="100%">motions</style></keyword><keyword><style  face="normal" font="default" size="100%">Science &amp; Technology - Other Topics</style></keyword><keyword><style  face="normal" font="default" size="100%">sensitivity</style></keyword><keyword><style  face="normal" font="default" size="100%">simulations</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Jan</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">5</style></volume><pages><style face="normal" font="default" size="100%">7</style></pages><isbn><style face="normal" font="default" size="100%">2041-1723</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Protein biological function depends on structural flexibility and change. From cellular communication through membrane ion channels to oxygen uptake and delivery by haemoglobin, structural changes are critical. It has been suggested that vibrations that extend through the protein play a crucial role in controlling these structural changes. While nature may utilize such long-range vibrations for optimization of biological processes, bench-top characterization of these extended structural motions for engineered biochemistry has been elusive. Here we show the first optical observation of long-range protein vibrational modes. This is achieved by orientation-sensitive terahertz near-field microscopy measurements of chicken egg white lysozyme single crystals. Underdamped modes are found to exist for frequencies &amp;gt;10 cm(-1). The existence of these persisting motions indicates that damping and intermode coupling are weaker than previously assumed. The methodology developed permits protein engineering based on dynamical network optimization.&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:000331084200018</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: AA4RQ&lt;br/&gt;Times Cited: 101&lt;br/&gt;Cited Reference Count: 48&lt;br/&gt;Cited References: &lt;br/&gt;     AUSTIN RH, 1989, PHYS REV LETT, V62, P1912, DOI 10.1103/PhysRevLett.62.1912&lt;br/&gt;     Bahar I, 2005, CURR OPIN STRUC BIOL, V15, P586, DOI 10.1016/j.sbi.2005.08.007&lt;br/&gt;     Balabin IA, 2000, SCIENCE, V290, P114, DOI 10.1126/science.290.5489.114&lt;br/&gt;     Balog E, 2004, PHYS REV LETT, V93, DOI 10.1103/PhysRevLett.93.028103&lt;br/&gt;     Barth A, 2002, Q REV BIOPHYS, V35, P369, DOI 10.1017/S0033583502003815&lt;br/&gt;     Benkovic SJ, 2003, SCIENCE, V301, P1196, DOI 10.1126/science.1085515&lt;br/&gt;     Brooks BR, 2009, J COMPUT CHEM, V30, P1545, DOI 10.1002/jcc.21287&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     Brooks CL, 1988, PROTEINS THEORETICAL&lt;br/&gt;     Chen JY, 2007, APPL PHYS LETT, V90, DOI 10.1063/1.2748852&lt;br/&gt;     Chen JY, 2005, PHYS REV E, V72, DOI 10.1103/PhysRevE.72.040901&lt;br/&gt;     Ding T, 2012, VIB SPECTROSC, V61, P144, DOI 10.1016/j.vibspec.2012.02.020&lt;br/&gt;     GENZEL L, 1976, BIOPOLYMERS, V15, P219, DOI 10.1002/bip.1976.360150115&lt;br/&gt;     George DK, 2013, IEEE T THZ SCI TECHN, V3, P288, DOI 10.1109/TTHZ.2013.2256233&lt;br/&gt;     GRISCHKOWSKY D, 1990, J OPT SOC AM B, V7, P2006, DOI 10.1364/JOSAB.7.002006&lt;br/&gt;     Hafner J, 2011, J CHEM PHYS, V135, DOI 10.1063/1.3646312&lt;br/&gt;     Hammes GG, 2002, BIOCHEMISTRY-US, V41, P8221, DOI 10.1021/bi0260839&lt;br/&gt;     He YF, 2011, BIOPHYS J, V100, P1058, DOI 10.1016/j.bpj.2010.12.3731&lt;br/&gt;     KACHALOVA GS, 1991, FEBS LETT, V284, P91, DOI 10.1016/0014-5793(91)80769-Y&lt;br/&gt;     Karplus M, 2005, P NATL ACAD SCI USA, V102, P6679, DOI 10.1073/pnas.0408930102&lt;br/&gt;     Knab J, 2006, BIOPHYS J, V90, P2576, DOI 10.1529/biophysj.105.069088&lt;br/&gt;     Knab JR, 2010, APPL PHYS LETT, V97, DOI 10.1063/1.3467192&lt;br/&gt;     LEVY RM, 1984, J PHYS CHEM-US, V88, P4233, DOI 10.1021/j150663a009&lt;br/&gt;     Lipps F, 2012, PHYS CHEM CHEM PHYS, V14, P6375, DOI 10.1039/c2cp23760a&lt;br/&gt;     Liu D, 2008, PHYS REV LETT, V101, DOI 10.1103/PhysRevLett.101.135501&lt;br/&gt;     MacKerell AD, 1998, J PHYS CHEM B, V102, P3586, DOI 10.1021/jp973084f&lt;br/&gt;     Markelz AG, 2008, IEEE J SEL TOP QUANT, V14, P180, DOI 10.1109/JSTQE.2007.913424&lt;br/&gt;     Meinhold L, 2007, PHYS REV LETT, V99, DOI 10.1103/PhysRevLett.99.138101&lt;br/&gt;     Meinhold L, 2007, PROTEINS, V66, P941, DOI 10.1002/prot.21246&lt;br/&gt;     Mittleman D.M., 2003, SENSING TERAHERTZ RA&lt;br/&gt;     MOELLER KD, 1992, BIOPHYS J, V61, P276, DOI 10.1016/S0006-3495(92)81834-9&lt;br/&gt;     Perutz MF, 1998, ANNU REV BIOPH BIOM, V27, P1, DOI 10.1146/annurev.biophys.27.1.1&lt;br/&gt;     Planken PCM, 2011, J INFRARED MILLIM TE, V32, P975, DOI 10.1007/s10762-011-9824-3&lt;br/&gt;     Rheinstadter MC, 2009, PHYS REV LETT, V103, DOI 10.1103/PhysRevLett.103.128104&lt;br/&gt;     Sakai K., 2005, TERAHERTZ OPTOELECTR&lt;br/&gt;     Schumacher M, 2002, NATURE, V417, P501, DOI 10.1038/417501a&lt;br/&gt;     Siegrist K, 2006, J AM CHEM SOC, V128, P5764, DOI 10.1021/ja058176u&lt;br/&gt;     Singh R, 2012, J PHYS CHEM A, V116, P10359, DOI 10.1021/jp307288r&lt;br/&gt;     SMITH J, 1990, J CHEM PHYS, V93, P2974, DOI 10.1063/1.458885&lt;br/&gt;     SMITH JC, 1991, Q REV BIOPHYS, V24, P227, DOI 10.1017/S0033583500003723&lt;br/&gt;     TEETER MM, 1990, J PHYS CHEM-US, V94, P8091, DOI 10.1021/j100384a021&lt;br/&gt;     TIDOR B, 1994, J MOL BIOL, V238, P405, DOI 10.1006/jmbi.1994.1300&lt;br/&gt;     Tych KM, 2011, J APPL CRYSTALLOGR, V44, P129, DOI 10.1107/S0021889810043372&lt;br/&gt;     Urabe H, 1998, BIOPHYS J, V74, P1533, DOI 10.1016/S0006-3495(98)77865-8&lt;br/&gt;     Walther M, 2003, CHEM PHYS, V288, P261, DOI 10.1016/S0301-0104(03)00031-4&lt;br/&gt;     WU Q, 1995, APPL PHYS LETT, V67, P3523, DOI 10.1063/1.114909&lt;br/&gt;     Xie AH, 2002, PHYS REV LETT, V88, DOI 10.1103/PhysRevLett.88.018102&lt;br/&gt;     Xu J, 2006, J PHYS CHEM B, V110, P24255, DOI 10.1021/jp064830w&lt;br/&gt;Acbas, Gheorghe Niessen, Katherine A. Snell, Edward H. Markelz, A. G.&lt;br/&gt;Snell, Edward/G-2055-2018&lt;br/&gt;Snell, Edward/0000-0001-8714-3191; Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;National Science Foundation MRIboolean AND2 grant [DBI2959989]&lt;br/&gt;We thank Yunfen He and Benjamin Keen for their assistance with calculations. All calculations performed using facilities provided by The Center for Computational Research, SUNY, Buffalo. We thank the National Science Foundation MRI boolean AND 2 grant DBI2959989 for support.&lt;br/&gt;101&lt;br/&gt;4&lt;br/&gt;108&lt;br/&gt;Nature publishing group&lt;br/&gt;London</style></notes><custom7><style face="normal" font="default" size="100%">3076</style></custom7><auth-address><style face="normal" font="default" size="100%">[Acbas, Gheorghe|Niessen, Katherine A.|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA. [Snell, Edward H.|Markelz, A. G.] SUNY Buffalo, Hauptman Woodward Med Res Inst, Dept Biol Struct, Buffalo, NY 14203 USA.&lt;br/&gt;Markelz, AG (corresponding author), SUNY Buffalo, Dept Phys, 239 Fronczak Hall, Buffalo, NY 14260 USA.&lt;br/&gt;amarkelz@buffalo.edu</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%">Acbas, G.</style></author><author><style face="normal" font="default" size="100%">Niessen, K. A.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</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><secondary-authors><author><style face="normal" font="default" size="100%">Betz, M.</style></author><author><style face="normal" font="default" size="100%">Elezzabi, A. Y.</style></author><author><style face="normal" font="default" size="100%">Song, J. J.</style></author><author><style face="normal" font="default" size="100%">Tsen, K. T.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">Measuring phonons in protein crystals</style></title><secondary-title><style face="normal" font="default" size="100%">Ultrafast Phenomena and Nanophotonics Xvii</style></secondary-title><tertiary-title><style face="normal" font="default" size="100%">Proceedings of SPIE</style></tertiary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">correlated motions</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">mode</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular crystals</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular vibrations</style></keyword><keyword><style  face="normal" font="default" size="100%">normal modes</style></keyword><keyword><style  face="normal" font="default" size="100%">phonons</style></keyword><keyword><style  face="normal" font="default" size="100%">protein dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Terahertz</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year></dates><publisher><style face="normal" font="default" size="100%">Spie-Int Soc Optical Engineering</style></publisher><pub-location><style face="normal" font="default" size="100%">Bellingham</style></pub-location><volume><style face="normal" font="default" size="100%">8623</style></volume><isbn><style face="normal" font="default" size="100%">978-0-8194-9392-7</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Using Terahertz near field microscopy we find orientation dependent narrow band absorption features for lysozyme crystals. Here we discuss identification of protein collective modes associated with the observed features. Using normal mode calculations we find good agreement with several of the measured features, suggesting that the modes arise from internal molecular motions and not crystal phonons. Such internal modes have been associated with protein function.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000322829300003</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BGG42&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 5&lt;br/&gt;Cited References: &lt;br/&gt;     Bahar I, 2005, CURR OPIN STRUC BIOL, V15, P586, DOI 10.1016/j.sbi.2005.08.007&lt;br/&gt;     BROOKS B, 1985, P NATL ACAD SCI USA, V82, P4995, DOI 10.1073/pnas.82.15.4995&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     Karplus M, 2005, P NATL ACAD SCI USA, V102, P6679, DOI 10.1073/pnas.0408930102&lt;br/&gt;     Planken PCM, 2011, J INFRARED MILLIM TE, V32, P975, DOI 10.1007/s10762-011-9824-3&lt;br/&gt;Acbas, Gheorghe Niessen, Katherine A. George, Deepu K. Snell, Edward Markelz, A. G.&lt;br/&gt;Proceedings Paper&lt;br/&gt;Conference on Ultrafast Phenomena and Nanophotonics XVII&lt;br/&gt;Feb 03-06, 2013&lt;br/&gt;San Francisco, CA&lt;br/&gt;SPIE, Femtolasers Inc&lt;br/&gt;Snell, Edward/G-2055-2018; George, Deepu/J-9882-2014&lt;br/&gt;Snell, Edward/0000-0001-8714-3191; George, Deepu/0000-0003-0021-0705; Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;National Science Foundation MRI2 [DBI2959989]&lt;br/&gt;We thank the National Science Foundation MRI2 grant DBI2959989 for support.&lt;br/&gt;1000 20th st, po box 10, bellingham, wa 98227-0010 usa&lt;br/&gt;0277-786x&lt;br/&gt;862305</style></notes><auth-address><style face="normal" font="default" size="100%">[Acbas, Gheorghe|Niessen, Katherine A.|George, Deepu K.|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA. [Snell, Edward] SUNY Buffalo, Dept Struct Biol, Buffalo, NY 14260 USA.&lt;br/&gt;Acbas, G (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.</style></auth-address></record></records></xml>