<?xml version="1.0" encoding="UTF-8"?><xml><records><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%">Niessen, K.</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%">Rapid Terahertz Dichroism Near Field Microscopy for Biomolecular Intramolecular Vibrational Spectroscopy</style></title><secondary-title><style face="normal" font="default" size="100%">APS 2018</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://meetings.aps.org/link/BAPS.2018.MAR.A50.8</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">A50.008</style></volume><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%">Xu, Mengyang</style></author><author><style face="normal" font="default" size="100%">Niessen, Katherine</style></author><author><style face="normal" font="default" size="100%">Deng, Yanting</style></author><author><style face="normal" font="default" size="100%">Michki, Nigel</style></author><author><style face="normal" font="default" size="100%">Snell, Edward</style></author><author><style face="normal" font="default" size="100%">Markelz, Andrea</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%"> The Role of Dynamical Transition in Protein Function: Coupling of Protein Collective Vibrations and Water Dynamics</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;Computational simulations have revealed protein collective vibrations prompt structural rearrangements to accomplish biological function. However, the biological importance of collective vibrations has not been experimentally demonstrated. The attempts have been hampered by the inability to distinguish localized water or side-chain relaxational motions from protein long-range vibrations using conventional techniques. The dynamical transition (DT), extensively observed using X-ray, neutron scattering, NMR and terahertz techniques [1,2], describes a rapid increase in the temperature-dependent dynamics of critically hydrated proteins above ∼220 K, and has been attributed to thermally activated solvent motions. While some proteins lose function below the specific temperature, others do not. We suggest the difference arises from the nature of the required motions for function. Specifically, functional motions enabled by long-range vibrations will be vulnerable to DT, which require surrounding solvent to be sufficiently mobile. We explored the coupling of protein vibrations to solvent dynamics by applying a recently developed technique, anisotropy terahertz microscopy [3], to directly measure the collective vibrations for lysozyme and investigate the temperature dependence in 150-300 K range. We find long-range intramolecular vibrations occur at 220K and rapidly increase in strength with increasing temperature, consistent with enhanced access above the DT. The results suggest collective vibrations are slaved to DT, and those proteins with function reliant on these motions will cease function below DT.&lt;/p&gt;

&lt;p&gt;1. Doster,W., et al. Phys.Rev.Lett., 2010.104(9):098101.&lt;/p&gt;

&lt;p&gt;2. Niessen,K., et al. Biophys.Rev., 2015.7,201.&lt;/p&gt;

&lt;p&gt;3. Acbas,G., et al. Nat.Commun., 2014.5,3076.&lt;/p&gt;
</style></abstract></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%">Liang, W.</style></author><author><style face="normal" font="default" size="100%">He, Y. F.</style></author><author><style face="normal" font="default" size="100%">George, D.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author></authors><secondary-authors><author><style face="normal" font="default" size="100%">Razeghi, M.</style></author><author><style face="normal" font="default" size="100%">Mohseni, H.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">The role of the protein surface on the local biological water dynamics</style></title><secondary-title><style face="normal" font="default" size="100%">Biosensing Ii</style></secondary-title><tertiary-title><style face="normal" font="default" size="100%">Proceedings of SPIE</style></tertiary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">alanine</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">hydration</style></keyword><keyword><style  face="normal" font="default" size="100%">lysine</style></keyword><keyword><style  face="normal" font="default" size="100%">lysozyme</style></keyword><keyword><style  face="normal" font="default" size="100%">proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">relaxation</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Terahertz</style></keyword><keyword><style  face="normal" font="default" size="100%">thz</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year></dates><publisher><style face="normal" font="default" size="100%">Spie-Int Soc Optical Engineering</style></publisher><pub-location><style face="normal" font="default" size="100%">Bellingham</style></pub-location><volume><style face="normal" font="default" size="100%">7397</style></volume><isbn><style face="normal" font="default" size="100%">978-0-8194-7687-6</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 function is reliant on structural flexibility and this flexibility is slaved to the surrounding solvent. Here we discuss how the exposed surface of the protein influences the solvent dynamics and thereby influences the protein&#039;s own structural dynamics. We discuss measurements of the THz absorption of water in the presence of hydrophilic and hydrophobic surfaces.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000292381700019</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BVQ85&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 12&lt;br/&gt;Cited References: &lt;br/&gt;     Balu R, 2008, BIOPHYS J, V94, P3217, DOI 10.1529/biophysj.107.105163&lt;br/&gt;     Bergner A, 2005, REV SCI INSTRUM, V76, DOI 10.1063/1.1928427&lt;br/&gt;     Born B, 2009, J AM CHEM SOC, V131, P3752, DOI 10.1021/ja808997y&lt;br/&gt;     Chen JY, 2007, APPL PHYS LETT, V90, DOI 10.1063/1.2748852&lt;br/&gt;     He YF, 2008, PHYS REV LETT, V101, DOI 10.1103/PhysRevLett.101.178103&lt;br/&gt;     Heugen U, 2006, P NATL ACAD SCI USA, V103, P12301, DOI 10.1073/pnas.0604897103&lt;br/&gt;     Jepsen PU, 2007, OPT EXPRESS, V15, P14717, DOI 10.1364/OE.15.014717&lt;br/&gt;     Kindt JT, 1996, J PHYS CHEM-US, V100, P10373, DOI 10.1021/jp960141g&lt;br/&gt;     Knab J, 2006, BIOPHYS J, V90, P2576, DOI 10.1529/biophysj.105.069088&lt;br/&gt;     THRANE L, 1995, CHEM PHYS LETT, V240, P330, DOI 10.1016/0009-2614(95)00543-D&lt;br/&gt;     Xu J, 2006, J CHEM PHYS, V124, DOI 10.1063/1.2151267&lt;br/&gt;     Yada H, 2008, CHEM PHYS LETT, V464, P166, DOI 10.1016/j.cplett.2008.09.015&lt;br/&gt;Liang, Wei He, Yunfen George, Deepu Markelz, A. 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