<?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%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Mittleman, D. M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Perspective on Terahertz Applications in Bioscience and Biotechnology</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%">2022</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://pubs.acs.org/doi/abs/10.1021/acsphotonics.2c00228</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">9</style></volume><pages><style face="normal" font="default" size="100%">1117-1126</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;Within the field of terahertz science and technology, one of the most active areas of current research focuses on the intersection of terahertz measurements and methods with the world of biology and medicine. Current activities revolve around numerous diverse questions, ranging from studies of the vibrational spectra of biomolecules and macromolecular complexes to biosensing to medical diagnostics based on noninvasive imaging techniques. Unlike many other areas in which terahertz science is now making inroads, this research domain has been plagued with a number of misleading ideas, which originated at least two decades ago and continue to crop up in current literature. In the worst case, these unfortunate notions can distract from, and even obscure, fascinating and meaningful results. The purpose of this Perspective is to highlight a few of these mistaken concepts and, more importantly, to distinguish them from the many interesting works that continue to emerge from the fruitful marriage of terahertz with biology and medicine.&lt;/p&gt;
</style></abstract><section><style face="normal" font="default" size="100%">1117</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%">M. Xu</style></author><author><style face="normal" font="default" size="100%">D. George</style></author><author><style face="normal" font="default" size="100%">R. Jimenez</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%">Photo-Switching of Protein Dynamical Collectivity</style></title><secondary-title><style face="normal" font="default" size="100%">Photonics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2021</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.mdpi.com/2304-6732/8/8/302</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">8</style></volume><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;We examine changes in the picosecond structural dynamics with irreversible photobleaching of red fluorescent proteins (RFP) mCherry, mOrange2 and TagRFP-T. Measurements of the protein dynamical transition using terahertz time-domain spectroscopy show in all cases an increase in the turn-on temperature in the bleached state. The result is surprising given that there is little change in the protein surface, and thus, the solvent dynamics held responsible for the transition should not change. A spectral analysis of the measurements guided by quasiharmonic calculations of the protein absorbance reveals that indeed the solvent dynamical turn-on temperature is independent of the thermal stability/photostate however the protein dynamical turn-on temperature shifts to higher temperatures. This is the first demonstration of switching the protein dynamical turn-on temperature with protein functional state. The observed shift in protein dynamical turn-on temperature relative to the solvent indicates an increase in the required mobile waters necessary for the protein picosecond motions, that is, these motions are more collective. Melting-point measurements reveal that the photobleached state is more thermally stable, and structural analysis of related RFP’s shows that there is an increase in internal water channels as well as a more uniform atomic root mean squared displacement. These observations are consistent with previous suggestions that water channels form with extended light excitation providing O&lt;sub&gt;2 &lt;/sub&gt;access to the chromophore and subsequent fluorescence loss. We report that these same channels increase internal coupling enhancing thermal stability and collectivity of the picosecond protein motions. The terahertz spectroscopic characterization of the protein and solvent dynamical onsets can be applied generally to measure changes in collectivity of protein motions.&lt;/p&gt;
</style></abstract><section><style face="normal" font="default" size="100%">302</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%">Romo, T. D.</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%">Persistent Protein Motions in a Rugged Energy Landscape Revealed by Normal Mode Ensemble Analysis</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Chemical Information and Modeling</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Chem Inf. Model.</style></alt-title><short-title><style face="normal" font="default" size="100%">J. Chem Inf. Model.J. Chem Inf. Model.</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Computer Science</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular-dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">Pharmacology &amp; Pharmacy</style></keyword><keyword><style  face="normal" font="default" size="100%">photoactive yellow protein</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">state</style></keyword><keyword><style  face="normal" font="default" size="100%">vibrational-modes</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%">Dec</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">12</style></number><volume><style face="normal" font="default" size="100%">60</style></volume><pages><style face="normal" font="default" size="100%">6419-6426</style></pages><isbn><style face="normal" font="default" size="100%">1549-9596</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Proteins are allosteric machines that couple motions at distinct, often distant, sites to control biological function. Low-frequency structural vibrations are a mechanism of this long-distance connection and are often used computationally to predict correlations, but experimentally identifying the vibrations associated with specific motions has proved challenging. Spectroscopy is an ideal tool to explore these excitations, but measurements have been largely unable to identify important frequency bands. The result is at odds with some previous calculations and raises the question what methods could successfully characterize protein structural vibrations. Here we show the lack of spectral structure arises in part from the variations in protein structure as the protein samples the energy landscape. However, by averaging over the energy landscape as sampled using an aggregate 18.5 mu s of all-atom molecular dynamics simulation of hen egg white lysozyme and normal-mode analyses, we find vibrations with large overlap with functional displacements are surprisingly concentrated in narrow frequency bands. These bands are not apparent in either the ensemble averaged vibrational density of states or isotropic absorption. However, in the case of the ensemble averaged anisotropic absorption, there is persistent spectral structure and overlap between this structure and the functional displacement frequency bands. We systematically lay out heuristics for calculating the spectra robustly, including the need for statistical sampling of the protein and inclusion of adequate water in the spectral calculation. The results show the congested spectrum of these complex molecules obscures important frequency bands associated with function and reveal a method to overcome this congestion by combining structurally sensitive spectroscopy with robust normal mode ensemble analysis.&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:000608875100076</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: PT8QA&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 47&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Bahar I, 2007, CURR OPIN STRUC BIOL, V17, P633, DOI 10.1016/j.sbi.2007.09.011&lt;br/&gt;     Balog E, 2011, J PHYS CHEM B, V115, P6811, DOI 10.1021/jp108493g&lt;br/&gt;     Castro-Camus E, 2008, CHEM PHYS LETT, V455, P289, DOI 10.1016/j.cplett.2008.02.084&lt;br/&gt;     Cerutti DS, 2008, BIOCHEMISTRY-US, V47, P12065, DOI 10.1021/bi800894u&lt;br/&gt;     Cerutti DS, 2019, WIRES COMPUT MOL SCI, V9, DOI 10.1002/wcms.1402&lt;br/&gt;     CHO M, 1994, J CHEM PHYS, V100, P6672, DOI 10.1063/1.467027&lt;br/&gt;     Choi JH, 2014, J PHYS CHEM B, V118, P12837, DOI 10.1021/jp508547y&lt;br/&gt;     Cote Y, 2017, BIOPHYS J, V112, P2575, DOI 10.1016/j.bpj.2017.05.018&lt;br/&gt;     Dong J, 1999, ACTA CRYSTALLOGR D, V55, P745, DOI 10.1107/S0907444998016047&lt;br/&gt;     ESSMANN U, 1995, J CHEM PHYS, V103, P8577, DOI 10.1063/1.470117&lt;br/&gt;     Falconer RJ, 2012, J INFRARED MILLIM TE, V33, P973, DOI 10.1007/s10762-012-9915-9&lt;br/&gt;     FELLER SE, 1995, J CHEM PHYS, V103, P4613, DOI 10.1063/1.470648&lt;br/&gt;     Gerek ZN, 2011, PLOS COMPUT BIOL, V7, DOI 10.1371/journal.pcbi.1002154&lt;br/&gt;     GO N, 1983, P NATL ACAD SCI-BIOL, V80, P3696, DOI 10.1073/pnas.80.12.3696&lt;br/&gt;     Grossfield A, 2019, LIVING J COMPUT MOL, V1, P5067, DOI DOI 10.33011/LIVEC0MS.1.1.5067&lt;br/&gt;     Grossfield A, 2009, ANN REP COMP CHEM, V5, P23, DOI 10.1016/S1574-1400(09)00502-7&lt;br/&gt;     He YF, 2011, BIOPHYS J, V100, P1058, DOI 10.1016/j.bpj.2010.12.3731&lt;br/&gt;     HORIUCHI T, 1991, PROTEINS, V10, P106, DOI 10.1002/prot.340100204&lt;br/&gt;     Huang J, 2013, J COMPUT CHEM, V34, P2135, DOI 10.1002/jcc.23354&lt;br/&gt;     Katebi AR, 2014, PROTEIN SCI, V23, P213, DOI 10.1002/pro.2407&lt;br/&gt;     Kindt JT, 1997, J CHEM PHYS, V106, P4389, DOI 10.1063/1.473486&lt;br/&gt;     Kroll J, 2007, VIB SPECTROSC, V43, P324, DOI 10.1016/j.vibspec.2006.03.010&lt;br/&gt;     Leioatts N, 2012, J CHEM THEORY COMPUT, V8, P2424, DOI 10.1021/ct3000316&lt;br/&gt;     Lerbret A, 2009, J CHEM PHYS, V131, DOI 10.1063/1.3273218&lt;br/&gt;     Meinhold L, 2007, PHYS REV LETT, V99, DOI 10.1103/PhysRevLett.99.138101&lt;br/&gt;     Miller DW, 1999, J MOL BIOL, V286, P267, DOI 10.1006/jmbi.1998.2445&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;     Phillips JC, 2005, J COMPUT CHEM, V26, P1781, DOI 10.1002/jcc.20289&lt;br/&gt;     Porter JR, 2019, BIOPHYS J, V116, P818, DOI 10.1016/j.bpj.2018.11.3144&lt;br/&gt;     Romo TD, 2014, J COMPUT CHEM, V35, P2305, DOI 10.1002/jcc.23753&lt;br/&gt;     Romo TD, 2009, IEEE ENG MED BIO, P2332, DOI 10.1109/IEMBS.2009.5335065&lt;br/&gt;     Sassi P, 2013, J CHEM PHYS, V139, DOI 10.1063/1.4838355&lt;br/&gt;     Singh R, 2012, J PHYS CHEM A, V116, P10359, DOI 10.1021/jp307288r&lt;br/&gt;     Stehle CU, 2012, J CHEM PHYS, V136, DOI 10.1063/1.3686886&lt;br/&gt;     STRAUB JE, 1994, J PHYS CHEM-US, V98, P10978, DOI 10.1021/j100093a046&lt;br/&gt;     Tehver R, 2009, J MOL BIOL, V387, P390, DOI 10.1016/j.jmb.2008.12.032&lt;br/&gt;     Thirumuruganandham SP, 2009, J MOL MODEL, V15, P959, DOI 10.1007/s00894-008-0446-1&lt;br/&gt;     Whitmire SE, 2003, BIOPHYS J, V85, P1269, DOI 10.1016/S0006-3495(03)74562-7&lt;br/&gt;     Xie AH, 2000, PHYS REV LETT, V84, P5435, DOI 10.1103/PhysRevLett.84.5435&lt;br/&gt;     Xu D, 1996, J PHYS CHEM-US, V100, P12108, DOI 10.1021/jp960076a&lt;br/&gt;     Yu X, 2005, J CHEM PHYS, V122, DOI 10.1063/1.1830431&lt;br/&gt;     Yu X, 2004, CHEM PHYS LETT, V391, P181, DOI 10.1016/j.cplett.2004.04.100&lt;br/&gt;     Zakaria HA, 2011, APPL SPECTROSC, V65, P260, DOI 10.1366/10-06162&lt;br/&gt;     Zhang HL, 2009, J MOL GRAPH MODEL, V27, P655, DOI 10.1016/j.jmgm.2008.10.005&lt;br/&gt;     Zorba A, 2019, P NATL ACAD SCI USA, V116, P13937, DOI 10.1073/pnas.1906024116&lt;br/&gt;Romo, Tod D. Grossfield, Alan Markelz, Andrea G.&lt;br/&gt;Grossfield, Alan/0000-0002-5877-2789&lt;br/&gt;National Science FoundationNational Science Foundation (NSF) [MCB 1616529]; U.S. Department of EnergyUnited States Department of Energy (DOE) [DESC0016317]&lt;br/&gt;Funding was provided by the National Science Foundation (MCB 1616529) and the U.S. Department of Energy (DESC0016317).&lt;br/&gt;&lt;br/&gt;1&lt;br/&gt;Amer chemical soc&lt;br/&gt;Washington&lt;br/&gt;1549-960x</style></notes><auth-address><style face="normal" font="default" size="100%">[Romo, Tod D.|Grossfield, Alan] Univ Rochester, Dept Biochem &amp; Biophys, Med Ctr, Rochester, NY 14642 USA. [Markelz, Andrea G.] Univ Buffalo SUNY, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Markelz, AG (corresponding author), Univ Buffalo SUNY, 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%">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%">Crossen, K.</style></author><author><style face="normal" font="default" size="100%">McKinney, J.</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%">Is the Protein Dynamical Transition useful?</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%">2020</style></year></dates><volume><style face="normal" font="default" size="100%">118</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">3</style></issue><section><style face="normal" font="default" size="100%">521a</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.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Jimenez, R.</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%">Photo Switching of Protein Dynamical Collectivity</style></title><secondary-title><style face="normal" font="default" size="100%">arXiv:1906.00893</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://arxiv.org/abs/1906.00893</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%">George, Deepu K</style></author><author><style face="normal" font="default" size="100%">Chen, Michael C</style></author><author><style face="normal" font="default" size="100%">Ferré-D’Amaré, Adrian R</style></author><author><style face="normal" font="default" size="100%">Snell, Edward H</style></author><author><style face="normal" font="default" size="100%">Cody, Vivian</style></author><author><style face="normal" font="default" size="100%">Pace, James</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%">Protein and RNA dynamical fingerprinting</style></title><secondary-title><style face="normal" font="default" size="100%">Nature communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><number><style face="normal" font="default" size="100%">1</style></number><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">1-10</style></pages><isbn><style face="normal" font="default" size="100%">2041-1723</style></isbn><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>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>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%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Jimenez, R.</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%">Probing the Stability of Fluorescent Proteins by Terahertz Spectroscopy</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%">dynamics</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;The higher transmission through tissues of long wavelength light motivates the development of fluorescent proteins with excitation shifted to the red. However red fluorescent proteins (RFPs) are more susceptible to photobleaching than their shorter wavelength counterparts. In particular RFPs are more susceptible to photobleaching [1]. A possible reason for this is a decrease in the structural stability of the beta barrel. Measurements of structural stability include atomic root mean squared displacement &amp;lt;x(2)&amp;gt; measured by the X-ray B-factor and neutron quasi elastic scattering. To date, X-ray measurements of RFP&#039;s do not indicate a structural stability change and systematic scattering studies have not been performed. Using THz dielectric response we examine if the picosecond structural flexibility decreases with increasing FP stability.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000378889200449</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: 7&lt;br/&gt;Cited References: &lt;br/&gt;     Dean KM, 2011, BIOPHYS J, V101, P961, DOI 10.1016/j.bpj.2011.06.055&lt;br/&gt;     He YF, 2011, BIOPHYS J, V100, P1058, DOI 10.1016/j.bpj.2010.12.3731&lt;br/&gt;     Helms V, 2007, CHEMPHYSCHEM, V8, P23, DOI 10.1002/cphc.200600298&lt;br/&gt;     Leu BM, 2008, BIOPHYS J, V95, P5874, DOI 10.1529/biophysj.108.138198&lt;br/&gt;     Markelz AG, 2007, CHEM PHYS LETT, V442, P413, DOI 10.1016/j.cplett.2007.05.080&lt;br/&gt;     Nagy A, 2004, THERMOCHIM ACTA, V410, P161, DOI 10.1016/S0040-6031(03)00397-6&lt;br/&gt;     Zaccai G, 2000, SCIENCE, V288, P1604, DOI 10.1126/science.288.5471.1604&lt;br/&gt;Xu, Mengyang George, D. K. Jimenez, R. 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;George, Deepu/J-9882-2014&lt;br/&gt;George, Deepu/0000-0003-0021-0705&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|George, D. K.|Markelz, A. G.] SUNY Buffalo, Buffalo, NY 14260 USA. [Jimenez, R.] Univ Colorado, Boulder, CO 80309 USA.&lt;br/&gt;Xu, MY (corresponding author), SUNY Buffalo, Buffalo, NY 14260 USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>5</ref-type><contributors><authors><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%">Protein Dielectric Response at Terahertz Frequencies: Correlated and Diffusive Contributions</style></title><secondary-title><style face="normal" font="default" size="100%">Terahertz Biomedical Science and Technology</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2014</style></year></dates><publisher><style face="normal" font="default" size="100%">Taylor and Francis </style></publisher><volume><style face="normal" font="default" size="100%">edited by Joo Huik Son </style></volume><language><style face="normal" font="default" size="100%">eng</style></language><section><style face="normal" font="default" size="100%">11</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%">George, Deepu K</style></author><author><style face="normal" font="default" size="100%">Knab, Joseph R</style></author><author><style face="normal" font="default" size="100%">He, Yunfen</style></author><author><style face="normal" font="default" size="100%">Kumauchi, Masato</style></author><author><style face="normal" font="default" size="100%">Birge, Robert R</style></author><author><style face="normal" font="default" size="100%">Hoff, Wouter D</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%">Photoactive yellow protein terahertz response: hydration, heating and intermediate states</style></title><secondary-title><style face="normal" font="default" size="100%">IEEE Transactions on Terahertz Science and Technology</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2013</style></year></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">3</style></volume><pages><style face="normal" font="default" size="100%">288-294</style></pages><isbn><style face="normal" font="default" size="100%">2156-342X</style></isbn><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%">Markelz, Andrea G.</style></author><author><style face="normal" font="default" size="100%">Knab, Joseph R.</style></author><author><style face="normal" font="default" size="100%">Chen, Jing Yin</style></author><author><style face="normal" font="default" size="100%">He, Yunfen</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protein dynamical transition in terahertz dielectric response</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Physics Letters</style></secondary-title><short-title><style face="normal" font="default" size="100%">Chemical Physics Letters</style></short-title></titles><dates><year><style  face="normal" font="default" size="100%">2007</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://www.sciencedirect.com/science/article/pii/S000926140700680X</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">442</style></volume><pages><style face="normal" font="default" size="100%">413 - 417</style></pages><isbn><style face="normal" font="default" size="100%">0009-2614</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The 200K protein dynamical transition is observed for the first time in the terahertz dielectric response. The complex dielectric permittivity ε=ε′+iε″ is determined in the 0.2–2.0THz and 80–294K ranges. ε″ has a linear temperature dependence up to 200K then sharply increases. The low temperature linear dependence in ε″ suggests anharmonicity for temperatures 80K&amp;lt;t&amp;lt;180k, challenging=&quot;&quot; the=&quot;&quot; assumed=&quot;&quot; harmonicity=&quot;&quot; below=&quot;&quot; 200k.=&quot;&quot; temperature=&quot;&quot; dependence=&quot;&quot; is=&quot;&quot; consistent=&quot;&quot; with=&quot;&quot; thermally=&quot;&quot; activated=&quot;&quot; sidechain=&quot;&quot; motions=&quot;&quot; and=&quot;&quot; shows=&quot;&quot; involved=&quot;&quot; in=&quot;&quot; dynamical=&quot;&quot; transition=&quot;&quot; extend=&quot;&quot; to=&quot;&quot; subpicosecond=&quot;&quot; time=&quot;&quot; scales.&amp;lt;=&quot;&quot; div=&quot;&quot;&amp;gt;&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue></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%">Knab, Joseph R</style></author><author><style face="normal" font="default" size="100%">Chen, Jing-Yin</style></author><author><style face="normal" font="default" size="100%">Ye, Shuji</style></author><author><style face="normal" font="default" size="100%">He, Yunfen</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%">Protein conformational dynamics measured with terahertz time domain spectroscopy</style></title><secondary-title><style face="normal" font="default" size="100%">2006 Joint 31st International Conference on Infrared Millimeter Waves and 14th International Conference on Teraherz Electronics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2006</style></year></dates><publisher><style face="normal" font="default" size="100%">IEEE</style></publisher><pages><style face="normal" font="default" size="100%">183-183</style></pages><isbn><style face="normal" font="default" size="100%">1424403995</style></isbn><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%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Knab, J. R.</style></author><author><style face="normal" font="default" size="100%">Chen, J. Y.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protein dynamics studies using terahertz dielectric response</style></title><secondary-title><style face="normal" font="default" size="100%">Abstracts of Papers of the American Chemical Society</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Abstr. Pap. Am. Chem. Soc.</style></alt-title><short-title><style face="normal" font="default" size="100%">Abstr. Pap. Am. Chem. Soc.Abstr. Pap. Am. Chem. Soc.</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Chemistry</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Aug</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">230</style></volume><pages><style face="normal" font="default" size="100%">U347-U348</style></pages><isbn><style face="normal" font="default" size="100%">0065-7727</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:000236797300675</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 032TJ&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 0&lt;br/&gt;Markelz, A. G. Knab, J. R. Chen, J. -Y.&lt;br/&gt;230th National Meeting of the American-Chemical-Society&lt;br/&gt;Aug 28-sep 01, 2005&lt;br/&gt;Washington, DC&lt;br/&gt;Amer Chem Soc&lt;br/&gt;&lt;br/&gt;2&lt;br/&gt;Amer chemical soc&lt;br/&gt;Washington</style></notes><auth-address><style face="normal" font="default" size="100%">SUNY Buffalo, Dept Phys, Buffalo, NY 14620 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%">Whitmire, S. E.</style></author><author><style face="normal" font="default" size="100%">Wolpert, D.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Hillebrecht, J. R.</style></author><author><style face="normal" font="default" size="100%">Galan, J.</style></author><author><style face="normal" font="default" size="100%">Birge, R. R.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protein flexibility and conformational state: A comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsin</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%">angstrom resolution</style></keyword><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword><keyword><style  face="normal" font="default" size="100%">dna</style></keyword><keyword><style  face="normal" font="default" size="100%">films</style></keyword><keyword><style  face="normal" font="default" size="100%">frequency</style></keyword><keyword><style  face="normal" font="default" size="100%">harmonic-analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">inelastic neutron-scattering</style></keyword><keyword><style  face="normal" font="default" size="100%">large systems</style></keyword><keyword><style  face="normal" font="default" size="100%">mixed basis</style></keyword><keyword><style  face="normal" font="default" size="100%">normal-modes</style></keyword><keyword><style  face="normal" font="default" size="100%">purple membranes</style></keyword><keyword><style  face="normal" font="default" size="100%">structural-changes</style></keyword><keyword><style  face="normal" font="default" size="100%">transform infrared-spectroscopy</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Aug</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><volume><style face="normal" font="default" size="100%">85</style></volume><pages><style face="normal" font="default" size="100%">1269-1277</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&gt;Far infrared ( FIR) spectral measurements of wild-type (WT) and D96N mutant bacteriorhodopsin thin films have been carried out using terahertz time domain spectroscopy as a function of hydration, temperature, and conformational state. The results are compared to calculated spectra generated via normal mode analyses using CHARMM. We find that the FIR absorbance is slowly increasing with frequency and without strong narrow features over the range of 2-60 cm(-1) and up to a resolution of 0.17 cm(-1). The broad absorption shifts in frequency with decreasing temperature as expected with a strongly anharmonic potential and in agreement with neutron inelastic scattering results. Decreasing hydration shifts the absorption to higher frequencies, possibly resulting from decreased coupling mediated by the interior water molecules. Ground-state FIR absorbances have nearly identical frequency dependence, with the mutant having less optical density than the WT. In the M state, the FIR absorbance of the WT increases whereas there is no change for D96N. These results represent the first measurement of FIR absorbance change as a function of conformational state.&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:000184428300052</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 705ZZ&lt;br/&gt;Times Cited: 117&lt;br/&gt;Cited Reference Count: 55&lt;br/&gt;Cited References: &lt;br/&gt;     AUSTIN RH, 1975, BIOCHEMISTRY-US, V14, P5355, DOI 10.1021/bi00695a021&lt;br/&gt;     Birge RR, 1996, J PHYS CHEM-US, V100, P9990, DOI 10.1021/jp953669e&lt;br/&gt;     BOUSCHE O, 1992, PHOTOCHEM PHOTOBIOL, V56, P1085, DOI 10.1111/j.1751-1097.1992.tb09732.x&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     BROOKS BR, 1995, J COMPUT CHEM, V16, P1522, DOI 10.1002/jcc.540161209&lt;br/&gt;     Brooks CL, 1988, PROTEINS THEORETICAL&lt;br/&gt;     Brucherseifer M, 2000, APPL PHYS LETT, V77, P4049, DOI 10.1063/1.1332415&lt;br/&gt;     Chen Q, 2001, J OPT SOC AM B, V18, P823, DOI 10.1364/JOSAB.18.000823&lt;br/&gt;     DENCHER NA, 1989, P NATL ACAD SCI USA, V86, P7876, DOI 10.1073/pnas.86.20.7876&lt;br/&gt;     Der A, 2001, BIOCHEMISTRY-MOSCOW+, V66, P1234, DOI 10.1023/A:1013179101782&lt;br/&gt;     Diehl M, 1997, BIOPHYS J, V73, P2726, DOI 10.1016/S0006-3495(97)78301-2&lt;br/&gt;     DOSTER W, 1989, NATURE, V337, P754, DOI 10.1038/337754a0&lt;br/&gt;     FERRAND M, 1993, P NATL ACAD SCI USA, V90, P9668, DOI 10.1073/pnas.90.20.9668&lt;br/&gt;     GENZEL L, 1984, SPECTROSCOPY BIOL MO, P609&lt;br/&gt;     GRISCHKOWSKY D, 1991, OSA PROC, V9, P9&lt;br/&gt;     Guilbert C, 1996, CHEM PHYS, V204, P327, DOI 10.1016/0301-0104(95)00293-6&lt;br/&gt;     Han PY, 2000, OPT LETT, V25, P242, DOI 10.1364/OL.25.000242&lt;br/&gt;     Hinsen K, 1998, PROTEINS, V33, P417, DOI 10.1002/(SICI)1097-0134(19981115)33:3&lt;417::AID-PROT10&gt;3.0.CO;2-8&lt;br/&gt;     JANEZIC D, 1995, J COMPUT CHEM, V16, P1543, DOI 10.1002/jcc.540161210&lt;br/&gt;     Kusnetzow A, 1999, BIOPHYS J, V76, P2370, DOI 10.1016/S0006-3495(99)77394-7&lt;br/&gt;     Lanyi JK, 1999, INT REV CYTOL, V187, P161, DOI 10.1016/S0074-7696(08)62418-3&lt;br/&gt;     Lanyi JK, 2001, TRENDS BIOTECHNOL, V19, P140, DOI 10.1016/S0167-7799(01)01576-1&lt;br/&gt;     LINDSAY SM, 1988, BIOPOLYMERS, V27, P1015, DOI 10.1002/bip.360270610&lt;br/&gt;     Lisy V, 1997, J BIOMOL STRUCT DYN, V14, P517, DOI 10.1080/07391102.1997.10508150&lt;br/&gt;     LONGBOTTOM C, 2002, POTENTIAL USES TERAH&lt;br/&gt;     Luecke H, 1999, SCIENCE, V286, P255, DOI 10.1126/science.286.5438.255&lt;br/&gt;     Luecke H, 1999, J MOL BIOL, V291, P899, DOI 10.1006/jmbi.1999.3027&lt;br/&gt;     MacKerell AD, 1998, J PHYS CHEM B, V102, P3586, DOI 10.1021/jp973084f&lt;br/&gt;     Markelz AG, 2000, CHEM PHYS LETT, V320, P42, DOI 10.1016/S0009-2614(00)00227-X&lt;br/&gt;     MCINTOSH AR, 1991, BIOPHYS J, V60, P1, DOI 10.1016/S0006-3495(91)82025-2&lt;br/&gt;     MOUAWAD L, 1993, BIOPOLYMERS, V33, P599, DOI 10.1002/bip.360330409&lt;br/&gt;     Mouawad L, 1996, J MOL BIOL, V258, P393, DOI 10.1006/jmbi.1996.0257&lt;br/&gt;     Nagel M, 2002, APPL PHYS LETT, V80, P154, DOI 10.1063/1.1428619&lt;br/&gt;     Oesterhelt D, 1974, Methods Enzymol, V31, P667&lt;br/&gt;     Palmo K, 1998, J COMPUT CHEM, V19, P754, DOI 10.1002/(SICI)1096-987X(199805)19:7&lt;754::AID-JCC6&gt;3.0.CO;2-P&lt;br/&gt;     PERAHIA D, 1995, COMPUT CHEM, V19, P241, DOI 10.1016/0097-8485(95)00011-G&lt;br/&gt;     Person W.B., 1982, VIBRATIONAL INTENSIT&lt;br/&gt;     Polavarapu P. 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Univ Connecticut, Dept Chem, Storrs, CT USA. Univ Connecticut, Dept Mol &amp; Cell Biol, Storrs, CT 06269 USA.&lt;br/&gt;Markelz, AG (corresponding author), SUNY 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%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Roitberg, A.</style></author><author><style face="normal" font="default" size="100%">Heilweil, E. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Pulsed terahertz spectroscopy of DNA, bovine serum albumin and collagen between 0.1 and 2.0 THz</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Physics Letters</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Chem. Phys. Lett.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">b-dna</style></keyword><keyword><style  face="normal" font="default" size="100%">Chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">films</style></keyword><keyword><style  face="normal" font="default" size="100%">modes</style></keyword><keyword><style  face="normal" font="default" size="100%">Physics</style></keyword><keyword><style  face="normal" font="default" size="100%">proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Mar</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1-2</style></number><volume><style face="normal" font="default" size="100%">320</style></volume><pages><style face="normal" font="default" size="100%">42-48</style></pages><isbn><style face="normal" font="default" size="100%">0009-2614</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 first use of pulsed terahertz spectroscopy to examine low-frequency collective vibrational modes of biomolecules. Broadband absorption increasing with frequency was observed for lyophilized powder samples of calf thymus DNA, bovine serum albumin and collagen in the 0.06-2.00 THz (2-67 cm(-1)) frequency range, suggesting that a large number of the low-frequency collective modes for these systems are IR active. Transmission measurements at room temperature showed increasing FIR absorption with hydration and denaturing. (C) 2000 published by Elsevier Science B.V. All rights reserved.&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:000086211200008</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 299RG&lt;br/&gt;Times Cited: 561&lt;br/&gt;Cited Reference Count: 24&lt;br/&gt;Cited References: &lt;br/&gt;     Cai Y, 1998, APPL PHYS LETT, V73, P444, DOI 10.1063/1.121894&lt;br/&gt;     CARTER DC, 1994, ADV PROTEIN CHEM, V45, P153&lt;br/&gt;     Chen EF, 1998, BIOCHEMISTRY-US, V37, P5589, DOI 10.1021/bi972369f&lt;br/&gt;     CHEVILLE RA, 1995, OPT LETT, V20, P1646, DOI 10.1364/OL.20.001646&lt;br/&gt;     FENG Y, 1991, PHYS REV A, V43, P1049, DOI 10.1103/PhysRevA.43.1049&lt;br/&gt;     Fraser R.D.B., 1973, CONFORMATION FIBROUS&lt;br/&gt;     Frushour B., 1975, ADV INFRARED RAMAN S, V1&lt;br/&gt;     GENZEL L, 1984, SPECTROSCOPY BIOL MO, P609&lt;br/&gt;     GRIEBENOW K, 1995, P NATL ACAD SCI USA, V92, P10969, DOI 10.1073/pnas.92.24.10969&lt;br/&gt;     HAYWARD S, 1995, ANNU REV PHYS CHEM, V46, P223, DOI 10.1146/annurev.pc.46.100195.001255&lt;br/&gt;     KATZENELLENBOGE.N, 1992, ULTRA WIDEBAND SHORT&lt;br/&gt;     Kindt JT, 1996, J PHYS CHEM-US, V100, P10373, DOI 10.1021/jp960141g&lt;br/&gt;     LINDSAY SM, 1988, BIOPOLYMERS, V27, P1015, DOI 10.1002/bip.360270610&lt;br/&gt;     Lisy V, 1997, J BIOMOL STRUCT DYN, V14, P517, DOI 10.1080/07391102.1997.10508150&lt;br/&gt;     Markelz AG, 1998, APPL PHYS LETT, V72, P2229, DOI 10.1063/1.121329&lt;br/&gt;     Nossal R. 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NIST, Div Biotechnol, Gaithersburg, MD 20899 USA. Lucent Technol, Mat Phys Res, Murray Hill, NJ 07974 USA.&lt;br/&gt;Markelz, AG (corresponding author), SUNY 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%">Allen, S. J.</style></author><author><style face="normal" font="default" size="100%">Craig, K.</style></author><author><style face="normal" font="default" size="100%">Felix, C. L.</style></author><author><style face="normal" font="default" size="100%">Guimaraes, P.</style></author><author><style face="normal" font="default" size="100%">Heyman, J. N.</style></author><author><style face="normal" font="default" size="100%">Kaminski, J. P.</style></author><author><style face="normal" font="default" size="100%">Keay, B. J.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Ramian, G.</style></author><author><style face="normal" font="default" size="100%">Scott, J. S.</style></author><author><style face="normal" font="default" size="100%">Sherwin, M. S.</style></author><author><style face="normal" font="default" size="100%">Campman, K. L.</style></author><author><style face="normal" font="default" size="100%">Hopkins, P. F.</style></author><author><style face="normal" font="default" size="100%">Gossard, A. C.</style></author><author><style face="normal" font="default" size="100%">Chow, D.</style></author><author><style face="normal" font="default" size="100%">Lui, M.</style></author><author><style face="normal" font="default" size="100%">Liu, T. Y.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">PROBING TERAHERTZ DYNAMICS IN SEMICONDUCTOR NANOSTRUCTURES WITH UCSB FREE-ELECTRON LASERS</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Luminescence</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">1994</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">60-1</style></volume><pages><style face="normal" font="default" size="100%">250-255</style></pages><isbn><style face="normal" font="default" size="100%">0022-2313</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The UCSB free-electron lasers provide kilowatts of continuously tunable radiation from 120 GHz to 4.8 THz. They have the most impact on terahertz science and technology that require a tunable, high power source to explore non-linear dynamics or that sacrifice incident power to recover the linear response of systems with very small cross-section. We describe three experiments that demonstrate the utility of these lasers in experiments on the terahertz dynamics of semiconductor nanostructures: (i) terahertz dynamics of resonant tunneling diodes, (ii) saturation spectroscopy of quantum wells and (iii) photon-assisted tunneling in superlattices.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:A1994NR36100065</style></accession-num><notes><style face="normal" font="default" size="100%">Sherwin, Mark S/Q-4762-2017; Guimaraes, Paulo Sergio Soares/B-6918-2012&lt;br/&gt;Sherwin, Mark S/0000-0002-3869-1893; Guimaraes, Paulo Sergio Soares/0000-0002-0113-2641; Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;1993 International Conference on Luminescence (ICL 93)&lt;br/&gt;Aug 09-13, 1993&lt;br/&gt;Univ connecticut, storrs, ct&lt;br/&gt;Univ connecticut; opt soc amer; amer phys soc; ieee, laser &amp; electro opt soc; int union pure &amp; appl phys; int sci fdn; univ connecticut res fdn&lt;br/&gt;3</style></notes></record></records></xml>