<?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%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Chen, J. Y.</style></author><author><style face="normal" font="default" size="100%">He, Yunfen</style></author><author><style face="normal" font="default" size="100%">Knab, J. 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%">Functional-State Dependence of Picosecond Protein Dynamics</style></title><secondary-title><style face="normal" font="default" size="100%">J. Phys. Chem. B</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%">11134-11140</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;We examine temperature-dependent picosecond dynamics of two benchmarking proteins lysozyme and cytochrome &lt;em&gt;c&lt;/em&gt; using temperature-dependent terahertz permittivity measurements. We find that a double Arrhenius temperature dependence with activation energies &lt;em&gt;E&lt;/em&gt;&lt;sub&gt;1&lt;/sub&gt; ∼ 0.1 kJ/mol and &lt;em&gt;E&lt;/em&gt;&lt;sub&gt;2&lt;/sub&gt; ∼ 10 kJ/mol fits the folded and ligand-free state response. The higher activation energy is consistent with the so-called protein dynamical transition associated with beta relaxations at the solvent–protein interface. The lower activation energy is consistent with correlated structural motions. When the structure is removed by denaturing, the lower-activation-energy process is no longer present. Additionally, the lower-activation-energy process is diminished with ligand binding but not for changes in the internal oxidation state. We suggest that the lower-energy activation process is associated with collective structural motions that are no longer accessible with denaturing or binding.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">40</style></issue><section><style face="normal" font="default" size="100%">11134</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%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">He, Y.</style></author><author><style face="normal" font="default" size="100%">Knab, J. 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%">Functional State Dependence of Picosecond Protein Dynamics</style></title><secondary-title><style face="normal" font="default" size="100%">arXiv:1105.4425</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2012</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://arxiv.org/0054394</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%">Balu, R.</style></author><author><style face="normal" font="default" size="100%">Zhang, H.</style></author><author><style face="normal" font="default" size="100%">Zukowski, E.</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%">Gregurick, S. K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Terahertz spectroscopy of bacteriorhodopsin and rhodopsin: Similarities and differences</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><keyword><style  face="normal" font="default" size="100%">bovine rhodopsin</style></keyword><keyword><style  face="normal" font="default" size="100%">conformational-changes</style></keyword><keyword><style  face="normal" font="default" size="100%">elastic</style></keyword><keyword><style  face="normal" font="default" size="100%">frequency normal-modes</style></keyword><keyword><style  face="normal" font="default" size="100%">light activation</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular-dynamics simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">neutron-scattering</style></keyword><keyword><style  face="normal" font="default" size="100%">protein-coupled receptors</style></keyword><keyword><style  face="normal" font="default" size="100%">transmembrane helices</style></keyword><keyword><style  face="normal" font="default" size="100%">vibrational-modes</style></keyword><keyword><style  face="normal" font="default" size="100%">wild-type</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Apr</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">8</style></number><volume><style face="normal" font="default" size="100%">94</style></volume><pages><style face="normal" font="default" size="100%">3217-3226</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;We studied the low-frequency terahertz spectroscopy of two photoactive protein systems, rhodopsin and bacteriorhodopsin, as a means to characterize collective low-frequency motions in helical transmembrane proteins. From this work, we found that the nature of the vibrational motions activated by terahertz radiation is surprisingly similar between these two structurally similar proteins. Specifically, at the lowest frequencies probed, the cytoplasmic loop regions of the proteins are highly active; and at the higher terahertz frequencies studied, the extracellular loop regions of the protein systems become vibrationally activated. In the case of bacteriorhodopsin, the calculated terahertz spectra are compared with the experimental terahertz signature. This work illustrates the importance of terahertz spectroscopy to identify vibrational degrees of freedom which correlate to known conformational changes in these proteins.&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:000254420100030</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 280IP&lt;br/&gt;Times Cited: 50&lt;br/&gt;Cited Reference Count: 72&lt;br/&gt;Cited References: &lt;br/&gt;     Abdulaev NG, 1998, P NATL ACAD SCI USA, V95, P12854, DOI 10.1073/pnas.95.22.12854&lt;br/&gt;     Alexandrov V, 2005, PROTEIN SCI, V14, P633, DOI 10.1110/ps.04882105&lt;br/&gt;     Alexiev U, 2003, J MOL BIOL, V328, P705, DOI 10.1016/S0022-2836(03)00326-7&lt;br/&gt;     Altenbach C, 2001, BIOCHEMISTRY-US, V40, P15493, DOI 10.1021/bi011545o&lt;br/&gt;     AMADEI A, 1993, PROTEINS, V17, P412, DOI 10.1002/prot.340170408&lt;br/&gt;     Balog E, 2004, PHYS REV LETT, V93, DOI 10.1103/PhysRevLett.93.028103&lt;br/&gt;     Beck M, 1998, BIOCHEMISTRY-US, V37, P7630, DOI 10.1021/bi9801560&lt;br/&gt;     Bizzarri AR, 2001, EUR BIOPHYS J BIOPHY, V30, P443, DOI 10.1007/s002490100167&lt;br/&gt;     BROOKS B, 1983, P NATL ACAD SCI-BIOL, V80, P6571, DOI 10.1073/pnas.80.21.6571&lt;br/&gt;     BROOKS BR, 1995, J COMPUT CHEM, V16, P1522, DOI 10.1002/jcc.540161209&lt;br/&gt;     Bu ZM, 2000, J MOL BIOL, V301, P525, DOI 10.1006/jmbi.2000.3978&lt;br/&gt;     Chen JY, 2005, PHYS REV E, V72, DOI 10.1103/PhysRevE.72.040901&lt;br/&gt;     Chen Q, 2001, J OPT SOC AM B, V18, P823, DOI 10.1364/JOSAB.18.000823&lt;br/&gt;     Chung HS, 2005, P NATL ACAD SCI USA, V102, P612, DOI 10.1073/pnas.0408646102&lt;br/&gt;     Crozier PS, 2003, J MOL BIOL, V333, P493, DOI 10.1016/j.jmb.2003.08.045&lt;br/&gt;     Farrens DL, 1996, SCIENCE, V274, P768, DOI 10.1126/science.274.5288.768&lt;br/&gt;     Filippovich S. 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Zhang, H. Zukowski, E. Chen, J. -Y. Markelz, A. G. Gregurick, S. K.&lt;br/&gt;Zhang, Hailiang/F-8325-2010&lt;br/&gt;Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;52&lt;br/&gt;&lt;br/&gt;27&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%">[Balu, R.|Zhang, H.|Zukowski, E.|Gregurick, S. K.] Univ Maryland, Dept Chem &amp; Biochem, Baltimore, MD 21250 USA. [Chen, J. -Y.|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Gregurick, SK (corresponding author), Univ Maryland, Dept Chem &amp; Biochem, Baltimore, MD 21250 USA.&lt;br/&gt;greguric@umbe.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%">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>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>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%">Cerne, 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%">Large oxidation dependence observed in terahertz dielectric response for cytochrome c</style></title><secondary-title><style face="normal" font="default" size="100%">Physical Review E</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Phys. Rev. E</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">absorption</style></keyword><keyword><style  face="normal" font="default" size="100%">binding</style></keyword><keyword><style  face="normal" font="default" size="100%">conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">dna</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">heart ferricytochrome-c</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%">protein flexibility</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">state</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%">Oct</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><volume><style face="normal" font="default" size="100%">72</style></volume><pages><style face="normal" font="default" size="100%">4</style></pages><isbn><style face="normal" font="default" size="100%">1539-3755</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 dielectric response is used to characterize the collective mode density of states for cytochrome c as a function of oxidation state and hydration using terahertz time domain spectroscopy. A strong absorbance and refractive index increase was observed with the oxidation. A simple phenomenological fitting using a continuous distribution of oscillators reproduces the frequency dependence of the complex dielectric response as well as demonstrates quantitative agreement with a uniform increase in either mode density or polarizability with oxidation in the 5-80 cm(-1) frequency range. Hydration dependence measurements find that a difference in the equilibrium water content for ferri and ferro cytochrome c is not sufficient to account for the large change in terahertz response. The large dielectric increase at terahertz frequencies with oxidation suggests either a significant global softening of the potential and/or a significant increase in polarizability with oxidation.&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:000232930600005</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 979GO&lt;br/&gt;Times Cited: 51&lt;br/&gt;Cited Reference Count: 29&lt;br/&gt;Cited References: &lt;br/&gt;     BERGHUIS AM, 1992, J MOL BIOL, V223, P959, DOI 10.1016/0022-2836(92)90255-I&lt;br/&gt;     BONE S, 1985, J MOL BIOL, V181, P323, DOI 10.1016/0022-2836(85)90096-8&lt;br/&gt;     BONE S, 1982, J MOL BIOL, V157, P571, DOI 10.1016/0022-2836(82)90477-6&lt;br/&gt;     BROOKS B, 1985, P NATL ACAD SCI USA, V82, P4995, DOI 10.1073/pnas.82.15.4995&lt;br/&gt;     Brucherseifer M, 2000, APPL PHYS LETT, V77, P4049, DOI 10.1063/1.1332415&lt;br/&gt;     Carlson HA, 2002, CURR OPIN CHEM BIOL, V6, P447, DOI 10.1016/S1367-5931(02)00341-1&lt;br/&gt;     CHEN JY, IN PRESS BIOPHYS J&lt;br/&gt;     CUSACK S, 1986, PHYSICA B &amp; C, V136, P256, DOI 10.1016/S0378-4363(86)80069-9&lt;br/&gt;     EDEN D, 1982, P NATL ACAD SCI-BIOL, V79, P815, DOI 10.1073/pnas.79.3.815&lt;br/&gt;     FROHWIRT EM, 1959, BIOPHYS J, V71, P570&lt;br/&gt;     Jackson J.D., 1975, CLASSICAL ELECTRODYN&lt;br/&gt;     KOPPENOL WH, 1982, J BIOL CHEM, V257, P4426&lt;br/&gt;     Kutteruf MR, 2003, CHEM PHYS LETT, V375, P337, DOI 10.1016/S0009-2614(03)00856-X&lt;br/&gt;     Markelz A, 2002, PHYS MED BIOL, V47, P3797, DOI 10.1088/0031-9155/47/21/318&lt;br/&gt;     Markelz AG, 2000, CHEM PHYS LETT, V320, P42, DOI 10.1016/S0009-2614(00)00227-X&lt;br/&gt;     Menikh A, 2004, BIOSENS BIOELECTRON, V20, P658, DOI 10.1016/j.bios.2004.03.006&lt;br/&gt;     Nagel M, 2002, APPL PHYS LETT, V80, P154, DOI 10.1063/1.1428619&lt;br/&gt;     PETHIG R, 1979, DIELECTRIC ELECTRONI&lt;br/&gt;     Qi PXR, 1996, BIOCHEMISTRY-US, V35, P12275, DOI 10.1021/bi961042w&lt;br/&gt;     RINGE D, 1985, PROG BIOPHYS MOL BIO, V45, P197, DOI 10.1016/0079-6107(85)90002-1&lt;br/&gt;     SHECHTER E, 1967, BIOPOLYMERS, V5, P788, DOI 10.1002/bip.1967.360050812&lt;br/&gt;     SIMONSON T, 1995, P NATL ACAD SCI USA, V92, P1082, DOI 10.1073/pnas.92.4.1082&lt;br/&gt;     SREENATHAN BR, 1971, BIOCHEM BIOPH RES CO, V42, P1122, DOI 10.1016/0006-291X(71)90021-0&lt;br/&gt;     Takano T., 1984, Methods and Applications in Crystallographic Computing. International Summer School on Crystallographic Computing, P262&lt;br/&gt;     TAKANO T, 1980, P NATL ACAD SCI-BIOL, V77, P6371, DOI 10.1073/pnas.77.11.6371&lt;br/&gt;     Whitmire SE, 2003, BIOPHYS J, V85, P1269, DOI 10.1016/S0006-3495(03)74562-7&lt;br/&gt;     WHITMIRE SE, 2003, SENSING SCI ELECT TE, V2&lt;br/&gt;     Yamamoto K, 2002, B CHEM SOC JPN, V75, P1083, DOI 10.1246/bcsj.75.1083&lt;br/&gt;     Zhang CF, 2004, J PHYS CHEM B, V108, P10077, DOI 10.1021/jp049933y&lt;br/&gt;Chen, JY Knab, JR Cerne, J Markelz, AG&lt;br/&gt;Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;52&lt;br/&gt;&lt;br/&gt;22&lt;br/&gt;Amer physical soc&lt;br/&gt;College pk&lt;br/&gt;1550-2376&lt;br/&gt;1</style></notes><custom7><style face="normal" font="default" size="100%">040901</style></custom7><auth-address><style face="normal" font="default" size="100%">SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Chen, JY (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%">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></records></xml>