<?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%">Xu, M. Y.</style></author><author><style face="normal" font="default" size="100%">Niessen, K. A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Michki, N. S.</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%">Escaping the Water Cage: Protein Intramolecular Vibrations and the Dynamical Transition</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%">2017</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%">112</style></volume><pages><style face="normal" font="default" size="100%">318A-318A</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:000402375600574</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: EW3DR&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 0&lt;br/&gt;Xu, Mengyang Niessen, Katherine A. Deng, Yanting Michki, Nigel S. Markelz, Andrea G.&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;NSFNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; DOEUnited States Department of Energy (DOE) [DE-SC0016317]&lt;br/&gt;This work was supported by NSF (DBI 1556359 and MCB 1616529), and DOE DE-SC0016317.&lt;br/&gt;&lt;br/&gt;7&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Xu, Mengyang|Niessen, Katherine A.|Deng, Yanting|Michki, Nigel S.|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY 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%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Xu, M. Y.</style></author><author><style face="normal" font="default" size="100%">Liu, H. J.</style></author><author><style face="normal" font="default" size="100%">Blankenship, R. E.</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%">Orange Carotenoid Protein Picosecond Dynamics Changes with Photo and Chemical Activation</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%">2017</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%">112</style></volume><pages><style face="normal" font="default" size="100%">441A-441A</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:000402375700177</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: EW3DS&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 3&lt;br/&gt;Cited References: &lt;br/&gt;     King JD, 2014, FEBS LETT, V588, P4561, DOI 10.1016/j.febslet.2014.10.024&lt;br/&gt;     Wilson A, 2006, PLANT CELL, V18, P992, DOI 10.1105/tpc.105.040121&lt;br/&gt;     Wilson A, 2008, P NATL ACAD SCI USA, V105, P12075, DOI 10.1073/pnas.0804636105&lt;br/&gt;Deng, Yanting Xu, Mengyang Liu, Haijun Blankenship, Robert E. Markelz, Andrea G.&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;Liu, Haijun/0000-0003-0537-0302&lt;br/&gt;&lt;br/&gt;14&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Xu, Mengyang|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Liu, Haijun|Blankenship, Robert E.] Washington Univ, Dept Biol, Campus Box 1137, St Louis, MO 63130 USA. [Liu, Haijun|Blankenship, Robert E.] Washington Univ, Dept Chem, St Louis, MO 63130 USA.</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%">Xu, M. Y.</style></author><author><style face="normal" font="default" size="100%">Niessen, K.</style></author><author><style face="normal" font="default" size="100%">Michki, N.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Snell, E.</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%">Anisotropic Absorption Measurements Reveal Protein Dynamical Transition in Intramolecular Vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">2016 41st International Conference on Infrared, Millimeter, and Terahertz Waves</style></secondary-title><tertiary-title><style face="normal" font="default" size="100%">International Conference on Infrared Millimeter and Terahertz Waves</style></tertiary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year></dates><publisher><style face="normal" font="default" size="100%">Ieee</style></publisher><pub-location><style face="normal" font="default" size="100%">New York</style></pub-location><isbn><style face="normal" font="default" size="100%">978-1-4673-8485-8</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Modeling has predicted that intramolecular structural vibrations enables proteins to access functionally important structural change. We show that the vibrational density of states and the isotropic absorption in the terahertz range are only weakly dependent on the protein functional state for several bench marking proteins. At the same time the direction of motions changes dramatically with functional state and with a resulting impact on the anisotropic absorption. Our anisotropic THz microscopy (ATM) measurements confirm this sensitivity. Here we apply the technique to the question of whether the protein dynamical transition (DT) is important to protein function. We find a strong anisotropic resonance at 70 cm(-1) rapidly increases in strength at temperatures above the DT. As these intramolecular vibrations enable protein structure to change conformation, the results suggest function will cease below DT for those proteins that require large scale conformational change.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000391406200009</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BG7KC&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 4&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Niessen K., 2015, BIOPHYSICAL REV&lt;br/&gt;     PETHIG R, 1995, PROTEIN SOLVENT INTE, P265&lt;br/&gt;     RUPLEY JA, 1991, ADV PROTEIN CHEM, V41, P37&lt;br/&gt;Xu, Mengyang Niessen, Katherine Michki, Nigel Deng, Yanting Snell, Edward Markelz, A. G.&lt;br/&gt;Irmmw-thz&lt;br/&gt;Proceedings Paper&lt;br/&gt;41st International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)&lt;br/&gt;Sep 25-30, 2016&lt;br/&gt;Copenhagen, DENMARK&lt;br/&gt;DTU, IEEE, QMC Instruments, Danish Ctr Laser Infrastructure, DTU Fotonik, Dept Photon Engn, ARL, Carl Sberg Fdn, AF Off Sci Res, Tech Univ Denmark, IEEE Microwave Theory &amp; Tech Soc, Azpect Photon, Ekspla, Hubner HF Syst Engn, I2S, Laser Quantum, Menlo Syst, Neaspec, Springer, TeraView, Virginia Diodes&lt;br/&gt;Snell, Edward/G-2055-2018&lt;br/&gt;Snell, Edward/0000-0001-8714-3191&lt;br/&gt;345 e 47th st, new york, ny 10017 usa&lt;br/&gt;2162-2027</style></notes><auth-address><style face="normal" font="default" size="100%">[Xu, Mengyang|Niessen, Katherine|Michki, Nigel|Deng, Yanting|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Snell, Edward] Hauptman Woodward Med Res Inst, Buffalo, NY USA.&lt;br/&gt;Xu, MY (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY USA.</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%">Xu, M. Y.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Jimenez, 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%">Probing the Stability of Fluorescent Proteins by Terahertz Spectroscopy</style></title><secondary-title><style face="normal" font="default" size="100%">2014 39th International Conference on Infrared, Millimeter, and Terahertz Waves</style></secondary-title><tertiary-title><style face="normal" font="default" size="100%">International Conference on Infrared Millimeter and Terahertz Waves</style></tertiary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year></dates><publisher><style face="normal" font="default" size="100%">Ieee</style></publisher><pub-location><style face="normal" font="default" size="100%">New York</style></pub-location><isbn><style face="normal" font="default" size="100%">978-1-4799-3877-3</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 higher transmission through tissues of long wavelength light motivates the development of fluorescent proteins with excitation shifted to the red. However red fluorescent proteins (RFPs) are more susceptible to photobleaching than their shorter wavelength counterparts. In particular RFPs are more susceptible to photobleaching [1]. A possible reason for this is a decrease in the structural stability of the beta barrel. Measurements of structural stability include atomic root mean squared displacement &amp;lt;x(2)&amp;gt; measured by the X-ray B-factor and neutron quasi elastic scattering. To date, X-ray measurements of RFP&#039;s do not indicate a structural stability change and systematic scattering studies have not been performed. Using THz dielectric response we examine if the picosecond structural flexibility decreases with increasing FP stability.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000378889200449</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BF0IL&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 7&lt;br/&gt;Cited References: &lt;br/&gt;     Dean KM, 2011, BIOPHYS J, V101, P961, DOI 10.1016/j.bpj.2011.06.055&lt;br/&gt;     He YF, 2011, BIOPHYS J, V100, P1058, DOI 10.1016/j.bpj.2010.12.3731&lt;br/&gt;     Helms V, 2007, CHEMPHYSCHEM, V8, P23, DOI 10.1002/cphc.200600298&lt;br/&gt;     Leu BM, 2008, BIOPHYS J, V95, P5874, DOI 10.1529/biophysj.108.138198&lt;br/&gt;     Markelz AG, 2007, CHEM PHYS LETT, V442, P413, DOI 10.1016/j.cplett.2007.05.080&lt;br/&gt;     Nagy A, 2004, THERMOCHIM ACTA, V410, P161, DOI 10.1016/S0040-6031(03)00397-6&lt;br/&gt;     Zaccai G, 2000, SCIENCE, V288, P1604, DOI 10.1126/science.288.5471.1604&lt;br/&gt;Xu, Mengyang George, D. K. Jimenez, R. Markelz, A. G.&lt;br/&gt;Irmmw-thz&lt;br/&gt;Proceedings Paper&lt;br/&gt;39th International Conference on Infrared, Millimeter, and Terahertz waves (IRMMW-THz)&lt;br/&gt;Sep 14-19, 2014&lt;br/&gt;Tucson, AZ&lt;br/&gt;THORLABS, Tydex, TOPTICA Photon, Bruker, Gentec EO, Lake Shore Cryotron, Ekspla, Zomega, TeraSense, Insight Product, Emcore, QMC Instruments, TeraView, NeaSpec, Advantest, MenloSystems, Traycer, Microtech Instruments Inc, LongWave Photon, Virginia Diodes Inc, ASU, MTT S, Journal Infrared Millimeter &amp; Tera Hertz Waves, Tera Hertz Sci &amp; Technol, Army Res Off&lt;br/&gt;George, Deepu/J-9882-2014&lt;br/&gt;George, Deepu/0000-0003-0021-0705&lt;br/&gt;345 e 47th st, new york, ny 10017 usa&lt;br/&gt;2162-2027</style></notes><auth-address><style face="normal" font="default" size="100%">[Xu, Mengyang|George, D. K.|Markelz, A. G.] SUNY Buffalo, Buffalo, NY 14260 USA. [Jimenez, R.] Univ Colorado, Boulder, CO 80309 USA.&lt;br/&gt;Xu, MY (corresponding author), SUNY Buffalo, Buffalo, NY 14260 USA.</style></auth-address></record></records></xml>