<?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%">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%">He, Yunfen</style></author><author><style face="normal" font="default" size="100%">Chen, J-Y</style></author><author><style face="normal" font="default" size="100%">Knab, Joseph R</style></author><author><style face="normal" font="default" size="100%">Zheng, Wenjun</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%">Evidence of protein collective motions on the picosecond timescale</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%">2011</style></year></dates><number><style face="normal" font="default" size="100%">4</style></number><volume><style face="normal" font="default" size="100%">100</style></volume><pages><style face="normal" font="default" size="100%">1058-1065</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language></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%">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%">The role of structure in the protein dynamical transition</style></title><secondary-title><style face="normal" font="default" size="100%">2008 33rd International Conference on Infrared, Millimeter and Terahertz Waves</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2008</style></year></dates><publisher><style face="normal" font="default" size="100%">IEEE</style></publisher><pages><style face="normal" font="default" size="100%">1-3</style></pages><isbn><style face="normal" font="default" size="100%">1424421195</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>17</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%">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%">Terahertz measurements of protein relaxational dynamics</style></title><secondary-title><style face="normal" font="default" size="100%">Proceedings of the IEEE</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2007</style></year></dates><number><style face="normal" font="default" size="100%">8</style></number><volume><style face="normal" font="default" size="100%">95</style></volume><pages><style face="normal" font="default" size="100%">1605-1610</style></pages><isbn><style face="normal" font="default" size="100%">0018-9219</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>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></records></xml>