<?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. 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. [Bandara, Sepalika|Ren, Zhong|Yang, Xiaojing] Univ Illinois, Dept Chem, Chicago, IL 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%">Ye, S. 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%">Hydration Effects on Energy Relaxation of Ferric Cytochrome C Films after Soret-Band Photoexcitation</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Physical Chemistry B</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Phys. Chem. B</style></alt-title><short-title><style face="normal" font="default" size="100%">J. Phys. Chem. BJ. Phys. Chem. B</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">circular-dichroism</style></keyword><keyword><style  face="normal" font="default" size="100%">conformation change</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">ferricytochrome-c</style></keyword><keyword><style  face="normal" font="default" size="100%">protein hydration</style></keyword><keyword><style  face="normal" font="default" size="100%">resolved resonance raman</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">unfolded states</style></keyword><keyword><style  face="normal" font="default" size="100%">vibrational-relaxation</style></keyword><keyword><style  face="normal" font="default" size="100%">water-molecules</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Nov</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">46</style></number><volume><style face="normal" font="default" size="100%">114</style></volume><pages><style face="normal" font="default" size="100%">15151-15157</style></pages><isbn><style face="normal" font="default" size="100%">1520-6106</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 hydration plays a critical role in protein dynamics and biological processes. Pump-probe transmission measurement has been applied to investigate the hydration effects on the energy relaxation of a heme protein ferric Cytochrome c (Cyt c) film after soret-band photoexcitation. Transient dynamics study indicates that the energy internal conversion time of similar to 300 fs is independent of hydration. The vibrationally excited electronic ground-state recovery rates show two transitions at the hydration level of h = 12.4-16.5% and 21.7-23.5%. The first transition occurs at the hydration level for the onset of an increasing ferric Cyt c flexibility while the second transition occurs at the saturated hydration level. The hydration dependence of steady-state electronic absorption spectrum results shows that the Q-band peak is nearly constant in center wavelength, but the line width surprisingly narrows with increasing hydration. For the similar to 695 nm absorbance associated with the MET80-Fe bond, the intensity increases with increasing hydration and slightly blue shifts. The 695 nm peak grows rapidly at h = 12.4% and then plateaus at h = 21.7%. This research shows that similar to 695 nm absorbance and ground-state recovery rates are sensitive to the hydration of the protein. This study will aid in understanding how hydration modulates the activity of the protein dynamics at a local level.&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:000284287700044</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 681CT&lt;br/&gt;Times Cited: 3&lt;br/&gt;Cited Reference Count: 87&lt;br/&gt;Cited References: &lt;br/&gt;     Bagchi B, 2005, CHEM REV, V105, P3197, DOI 10.1021/cr020661+&lt;br/&gt;     BAI YW, 1995, SCIENCE, V269, P192, DOI 10.1126/science.7618079&lt;br/&gt;     Bertini I, 2000, J MAGN RESON, V147, P1, DOI 10.1006/jmre.2000.2131&lt;br/&gt;     Bizzarri AR, 2002, J PHYS CHEM B, V106, P6617, DOI 10.1021/jp020100m&lt;br/&gt;     BONE S, 1985, J MOL BIOL, V181, P323, DOI 10.1016/0022-2836(85)90096-8&lt;br/&gt;     Bone S, 2008, J PHYS CHEM B, V112, P10071, DOI 10.1021/jp8009782&lt;br/&gt;     BULL HB, 1968, ARCH BIOCHEM BIOPHYS, V128, P488, DOI 10.1016/0003-9861(68)90055-6&lt;br/&gt;     BULL HB, 1970, ARCH BIOCHEM BIOPHYS, V137, P299, DOI 10.1016/0003-9861(70)90443-1&lt;br/&gt;     CHAMPION PM, 1981, J CHEM PHYS, V75, P490, DOI 10.1063/1.441846&lt;br/&gt;     Chen EF, 1999, J AM CHEM SOC, V121, P3811, DOI 10.1021/ja983169+&lt;br/&gt;     Chen JY, 2005, PHYS REV E, V72, DOI 10.1103/PhysRevE.72.040901&lt;br/&gt;     Cianetti S, 2004, J AM CHEM SOC, V126, P13932, DOI 10.1021/ja046442i&lt;br/&gt;     Dragomir I, 2007, BIOPHYS J, V92, P989, DOI 10.1529/biophysj.106.095976&lt;br/&gt;     Eaton W A, 1981, Methods Enzymol, V76, P175&lt;br/&gt;     EATON WA, 1967, J CHEM PHYS, V46, P2533, DOI 10.1063/1.1841081&lt;br/&gt;     EATON WA, 1968, J CHEM PHYS, V49, P985, DOI 10.1063/1.1670263&lt;br/&gt;     Ehrler OT, 2009, ACCOUNTS CHEM RES, V42, P769, DOI 10.1021/ar800263z&lt;br/&gt;     FERRAND M, 1993, P NATL ACAD SCI USA, V90, P9668, DOI 10.1073/pnas.90.20.9668&lt;br/&gt;     GASCOYNE PRC, 1977, J CHEM SOC FARAD T 1, V73, P171, DOI 10.1039/f19777300171&lt;br/&gt;     GIBSON QH, 1957, NATURE, V180, P1416, DOI 10.1038/1801416b0&lt;br/&gt;     Gregory R.B., 1995, PROTEIN SOLVENT INTE&lt;br/&gt;     HALLE B, 1981, J AM CHEM SOC, V103, P500, DOI 10.1021/ja00393a004&lt;br/&gt;     Halle B, 2004, PHILOS T R SOC B, V359, P1207, DOI 10.1098/rstb.2004.1499&lt;br/&gt;     Henchman RH, 2002, PROTEIN SCI, V11, P2080, DOI 10.1110/ps.0214002&lt;br/&gt;     Hertel IV, 2006, REP PROG PHYS, V69, P1897, DOI 10.1088/0034-4885/69/6/R06&lt;br/&gt;     Jayaram B, 2004, ANNU REV BIOPH BIOM, V33, P343, DOI 10.1146/annurev.biophys.33.110502.140414&lt;br/&gt;     Jimenez R, 2002, J PHYS CHEM B, V106, P9172, DOI 10.1021/jp0209648&lt;br/&gt;     JONES CM, 1993, P NATL ACAD SCI USA, V90, P11860, DOI 10.1073/pnas.90.24.11860&lt;br/&gt;     Joti Y, 2008, BIOPHYS J, V94, P4435, DOI 10.1529/biophysj.107.118042&lt;br/&gt;     Jougeward K. 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[Markelz, Andrea] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Ye, SJ (corresponding author), Univ Sci &amp; Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China.&lt;br/&gt;shujiye@ustc.edu.cn|amarkelz@buffalo.edu</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%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Chen, J.-Y.</style></author><author><style face="normal" font="default" size="100%">Knab, J. R.</style></author><author><style face="normal" font="default" size="100%">He, Y.</style></author><author><style face="normal" font="default" size="100%">Ye, S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Development of Tagless Biosensors for Detecting the Presence of Pathogens</style></title><secondary-title><style face="normal" font="default" size="100%">Terahertz Frequency Detection and Identification of Materials and Objects</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2007</style></year></dates><publisher><style face="normal" font="default" size="100%">Springer</style></publisher><pub-location><style face="normal" font="default" size="100%">Dordrecht, The Netherlands</style></pub-location><volume><style face="normal" font="default" size="100%">ed X.-C. Zhang, R. E. Miles, H. Eisele and A. Krotkus</style></volume><pages><style face="normal" font="default" size="100%">123-134</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><section><style face="normal" font="default" size="100%">9</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%">Chen, J. Y.</style></author><author><style face="normal" font="default" size="100%">Knab, J. R.</style></author><author><style face="normal" font="default" size="100%">Ye, S. J.</style></author><author><style face="normal" font="default" size="100%">He, Y. F.</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 dielectric assay of solution phase protein binding</style></title><secondary-title><style face="normal" font="default" size="100%">Applied Physics Letters</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Appl. Phys. Lett.</style></alt-title><short-title><style face="normal" font="default" size="100%">Appl. Phys. Lett.Appl. Phys. Lett.</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">lysozyme</style></keyword><keyword><style  face="normal" font="default" size="100%">Physics</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">water</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</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%">24</style></number><volume><style face="normal" font="default" size="100%">90</style></volume><pages><style face="normal" font="default" size="100%">3</style></pages><isbn><style face="normal" font="default" size="100%">0003-6951</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 authors demonstrate a method for rapid determination of protein-ligand binding on solution phase samples using terahertz dielectric spectroscopy. Measurements were performed using terahertz time domain spectroscopy on aqueous solutions below the liquid-solid transition for water. Small ligand binding sensitivity was demonstrated using triacetylglucosamine and hen egg white lysozyme with a decrease in dielectric response with binding. The magnitude of the change increases with frequency. (c) 2007 American Institute of Physics.&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:000247305400108</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 179QR&lt;br/&gt;Times Cited: 51&lt;br/&gt;Cited Reference Count: 9&lt;br/&gt;Cited References: &lt;br/&gt;     Balog E, 2004, PHYS REV LETT, V93, DOI 10.1103/PhysRevLett.93.028103&lt;br/&gt;     Brucherseifer M, 2000, APPL PHYS LETT, V77, P4049, DOI 10.1063/1.1332415&lt;br/&gt;     Chen JY, 2005, PHYS REV E, V72, DOI 10.1103/PhysRevE.72.040901&lt;br/&gt;     Fear G, 2007, PHARMACOL THERAPEUT, V113, P354, DOI 10.1016/j.pharmthera.2006.09.001&lt;br/&gt;     Heugen U, 2006, P NATL ACAD SCI USA, V103, P12301, DOI 10.1073/pnas.0604897103&lt;br/&gt;     Knab J, 2006, BIOPHYS J, V90, P2576, DOI 10.1529/biophysj.105.069088&lt;br/&gt;     LEHRER SS, 1967, J BIOL CHEM, V242, P4644&lt;br/&gt;     Menikh A, 2004, BIOSENS BIOELECTRON, V20, P658, DOI 10.1016/j.bios.2004.03.006&lt;br/&gt;     Xu J, 2006, PROTEIN SCI, V15, P1175, DOI 10.1110/ps.062073506&lt;br/&gt;Chen, Jing-Yin Knab, J. R. Ye, Shuji He, Yunfen Markelz, A. G.&lt;br/&gt;Ye, Shuji/B-4479-2010&lt;br/&gt;Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;53&lt;br/&gt;1&lt;br/&gt;42&lt;br/&gt;Amer inst physics&lt;br/&gt;Melville&lt;br/&gt;1077-3118</style></notes><custom7><style face="normal" font="default" size="100%">243901</style></custom7><auth-address><style face="normal" font="default" size="100%">SUNY Buffalo, Dept Phys, Buffalo, NY 14260 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%">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%">Kabir, N. A.</style></author><author><style face="normal" font="default" size="100%">Yoon, Y.</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><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Reno, J. L.</style></author><author><style face="normal" font="default" size="100%">Sadofyev, Y.</style></author><author><style face="normal" font="default" size="100%">Johnson, S.</style></author><author><style face="normal" font="default" size="100%">Zhang, Y. H.</style></author><author><style face="normal" font="default" size="100%">Bird, J. P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Terahertz transmission characteristics of high-mobility GaAs and InAs two-dimensional-electron-gas systems</style></title><secondary-title><style face="normal" font="default" size="100%">Applied Physics Letters</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Appl. Phys. Lett.</style></alt-title><short-title><style face="normal" font="default" size="100%">Appl. Phys. Lett.Appl. Phys. Lett.</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">field-effect transistors</style></keyword><keyword><style  face="normal" font="default" size="100%">photoconductivity</style></keyword><keyword><style  face="normal" font="default" size="100%">Physics</style></keyword><keyword><style  face="normal" font="default" size="100%">plasma-waves</style></keyword><keyword><style  face="normal" font="default" size="100%">radiation</style></keyword><keyword><style  face="normal" font="default" size="100%">resonant detection</style></keyword><keyword><style  face="normal" font="default" size="100%">subterahertz</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</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%">13</style></number><volume><style face="normal" font="default" size="100%">89</style></volume><pages><style face="normal" font="default" size="100%">3</style></pages><isbn><style face="normal" font="default" size="100%">0003-6951</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Frequency-dependent complex conductivity of high-mobility GaAs and InAs two-dimensional-electron-gas (2DEG) systems is studied by terahertz time domain spectroscopy. Determining the momentum relaxation time from a Drude model, the authors find a lower value than that from dc measurements, particularly at high frequencies/low temperatures. These deviations are consistent with the ratio tau(t)/tau(q,) where tau(q) is the full scattering time. This suggests that small-angle scattering leads to weaker heating of 2DEGs at low temperatures than expected from dc mobilit9y. (c) 2006 American Institute of Physics.&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:000240875800066</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 089JE&lt;br/&gt;Times Cited: 18&lt;br/&gt;Cited Reference Count: 16&lt;br/&gt;Cited References: &lt;br/&gt;     ANDO T, 1982, REV MOD PHYS, V54, P437, DOI 10.1103/RevModPhys.54.437&lt;br/&gt;     ANDO T, 1989, HIGH MAGNETIC FIELDS, V2, P164&lt;br/&gt;     Ashcroft NW, 1976, SOLID STATE PHYS, P1&lt;br/&gt;     Beard MC, 2000, PHYS REV B, V62, P15764, DOI 10.1103/PhysRevB.62.15764&lt;br/&gt;     Cerne J, 2000, PHYS REV B, V61, P8133, DOI 10.1103/PhysRevB.61.8133&lt;br/&gt;     COLERIDGE PT, 1991, PHYS REV B, V44, P3793, DOI 10.1103/PhysRevB.44.3793&lt;br/&gt;     Dorozhkin PS, 2005, APPL PHYS LETT, V87, DOI 10.1063/1.2035883&lt;br/&gt;     Knap W, 2002, APPL PHYS LETT, V81, P4637, DOI 10.1063/1.1525851&lt;br/&gt;     Knap W, 2002, APPL PHYS LETT, V80, P3433, DOI 10.1063/1.1473685&lt;br/&gt;     Kukushkin IV, 2005, APPL PHYS LETT, V86, DOI 10.1063/1.1856143&lt;br/&gt;     MADELUNG O, 1996, SEMICONDUCTORS BASIC, P109&lt;br/&gt;     MCKNIGHT SW, 1987, INFRARED PHYS, V27, P327, DOI 10.1016/0020-0891(87)90074-1&lt;br/&gt;     Peralta XG, 2002, APPL PHYS LETT, V81, P1627, DOI 10.1063/1.1497433&lt;br/&gt;     Sadofyev YG, 2002, APPL PHYS LETT, V81, P1833, DOI 10.1063/1.1504882&lt;br/&gt;     Shaner EA, 2005, APPL PHYS LETT, V87, DOI 10.1063/1.2128057&lt;br/&gt;     ZAWADZKI W, 1974, ADV PHYS, V23, P435, DOI 10.1080/00018737400101371&lt;br/&gt;Kabir, N. A. Yoon, Y. Knab, J. R. Chen, J. -Y. Markelz, A. G. Reno, J. L. Sadofyev, Y. Johnson, S. Zhang, Y. -H. Bird, J. P.&lt;br/&gt;Bird, Jonathan P/G-4068-2010&lt;br/&gt;Bird, Jonathan P/0000-0002-6966-9007; Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;18&lt;br/&gt;&lt;br/&gt;15&lt;br/&gt;Amer inst physics&lt;br/&gt;Melville</style></notes><custom7><style face="normal" font="default" size="100%">132109</style></custom7><auth-address><style face="normal" font="default" size="100%">SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA. SUNY Buffalo, Dept Elect Engn, Buffalo, NY 14260 USA. Sandia Natl Labs, Nanostruct &amp; Semicond Phys Dept, Albuquerque, NM 87185 USA. Arizona State Univ, Dept Elect Engn, Tempe, AZ 85287 USA. Arizona State Univ, Ctr Solid State Elect Res, Tempe, AZ 85287 USA.&lt;br/&gt;Markelz, AG (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;jbird@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%">Ye, S.</style></author><author><style face="normal" font="default" size="100%">Knab, J.</style></author><author><style face="normal" font="default" size="100%">Chen, J.-Y.</style></author><author><style face="normal" font="default" size="100%">Wang, S.</style></author><author><style face="normal" font="default" size="100%">Cheon, M.</style></author><author><style face="normal" font="default" size="100%">Luo, 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%">Ultrafast Carriers Dynamics in GaSb/Mn Random Alloys</style></title><secondary-title><style face="normal" font="default" size="100%">Proceedings of the 28th International Conference on the Physics of Semiconductors</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2006</style></year></dates><pub-location><style face="normal" font="default" size="100%">Vienna Austria</style></pub-location><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%">Chen, J.-Y.</style></author><author><style face="normal" font="default" size="100%">Knab, J. R.</style></author><author><style face="normal" font="default" size="100%">Ye, S.</style></author><author><style face="normal" font="default" size="100%">He, 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%">Using terahertz spectroscopy as a protein binding assay</style></title><secondary-title><style face="normal" font="default" size="100%"> Advanced Biomedical and Clinical Diagnostic Systems IV;</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">02/2006</style></date></pub-dates></dates><pub-location><style face="normal" font="default" size="100%"> San Jose, California, United States</style></pub-location><volume><style face="normal" font="default" size="100%">Proc SPIE 6080,</style></volume><pages><style face="normal" font="default" size="100%">35-42</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The vibrational modes corresponding to protein tertiary structural motion lay in the far infrared or terahertz frequency range. These collective large scale motions depend on global structure and thus will necessarily be perturbed by ligand binding events. We discuss the use of terahertz dielectric spectroscopy to measure these vibrational modes and the sensitivity of the technique to changes in protein conformation, oxidation state and environment. A challenge of applying this sensitivity as a spectroscopic assay for ligand binding is the sensitivity of the technique to both bulk water and water bound to the protein. This sensitivity can entirely obscure the signal from the protein or protein-ligand complex itself, thus necessitating sophisticated sample preparation making the technique impractical for industrial applications. We discuss methods to overcome this background and demonstrate how terahertz spectroscopy can be used to quickly assay protein binding for proteomics and pharmaceutical research.&lt;/p&gt;</style></abstract></record></records></xml>