<?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%">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%">Deng, Yanting</style></author><author><style face="normal" font="default" size="100%">Snell, Edward H.</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%">Importance of Protein Vibration Directionality on Function</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb 3</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">112</style></volume><pages><style face="normal" font="default" size="100%">353A-353A</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><accession-num><style face="normal" font="default" size="100%">WOS:000402375600746</style></accession-num><notes><style face="normal" font="default" size="100%">Snell, Edward/G-2055-2018&lt;br/&gt;Snell, Edward/0000-0001-8714-3191&lt;br/&gt;1&lt;br/&gt;58th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2014&lt;br/&gt;San Francisco, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;</style></notes></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, Yanting</style></author><author><style face="normal" font="default" size="100%">Xu, Mengyang</style></author><author><style face="normal" font="default" size="100%">Niessen, Katherine A.</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%">Direct Measurements of the Long-Range Collective Vibrations of Photoactive Yellow Protein</style></title><secondary-title><style face="normal" font="default" size="100%">30th Anniversary Symposium of The Protein Society</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://onlinelibrary.wiley.com/doi/10.1002/pro.3026</style></url></web-urls></urls><pub-location><style face="normal" font="default" size="100%">Baltimore MD</style></pub-location><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;Long-range collective vibrations are thought to be crucial to protein functions. In the case of photoactive protein family, modeling suggests the intramolecular vibrations provide an efficient means of energy relaxation[1], feedback for enhancement of chromophore vibrations that promote structural transitions[2] and can assist in charge energy transfer[3]. As a paradigm of this family, photoactive yellow protein (PYP) is a cytoplasmic photocycling protein related to negative phototactic response to blue light in purple photosynthetic bacteria. PYP has a p-coumaric acid chromophore binding to the cysteine residue via a thioester bond, whose vibrations were found to overlap calculated vibrations of the protein scaffold. Using our unique technique of anisotropic terahertz microscopy(ATM)[4], we measure the intramolecular vibrations for PYP for the first time, including cycling between ground and blue shift (pB) states. Room temperature ATM measurements are performed in the dark and with continuous wave illumination at 488nm, resulting in a steady pB state with approximately 5% population conversion. In pB state, we find an overall decrease in the strength of resonant band in frequency range of 30-60 cm-1. Our calculated spectra using quasi-harmonic analysis indicate that our measurements are dominated by the protein vibrations, rather than the pCA chromophore, allowing us to characterize how the scaffold dynamics changes with functional states and mutations.&lt;/p&gt;

&lt;p&gt;1. Levantino, M., et al. Nat Commun, 2015. 6.&lt;/p&gt;

&lt;p&gt;2. Mataga, N., et al. Chem. Phys. Lett., 2002. 352(3-4): p. 220-225.&lt;/p&gt;

&lt;p&gt;3. Fokas, A.S., et al. Photosynth. Res., 2014. 122&lt;/p&gt;
</style></abstract></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></records></xml>