<?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%">Lipps, F.</style></author><author><style face="normal" font="default" size="100%">Levy, 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%">Hydration and temperature interdependence of protein picosecond dynamics</style></title><secondary-title><style face="normal" font="default" size="100%">Physical Chemistry Chemical Physics</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Phys. Chem. Chem. Phys.</style></alt-title><short-title><style face="normal" font="default" size="100%">Phys. Chem. Chem. Phys.Phys. Chem. Chem. Phys.</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">dielectric-relaxation</style></keyword><keyword><style  face="normal" font="default" size="100%">fluctuations</style></keyword><keyword><style  face="normal" font="default" size="100%">inelastic neutron-scattering</style></keyword><keyword><style  face="normal" font="default" size="100%">lysozyme</style></keyword><keyword><style  face="normal" font="default" size="100%">myoglobin</style></keyword><keyword><style  face="normal" font="default" size="100%">percolation</style></keyword><keyword><style  face="normal" font="default" size="100%">Physics</style></keyword><keyword><style  face="normal" font="default" size="100%">spectra</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">terahertz beams</style></keyword><keyword><style  face="normal" font="default" size="100%">transition</style></keyword><keyword><style  face="normal" font="default" size="100%">water</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year></dates><number><style face="normal" font="default" size="100%">18</style></number><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">6375-6381</style></pages><isbn><style face="normal" font="default" size="100%">1463-9076</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 investigate the nature of the solvent motions giving rise to the rapid temperature dependence of protein picoseconds motions at 220 K, often referred to as the protein dynamical transition. The interdependence of picoseconds dynamics on hydration and temperature is examined using terahertz time domain spectroscopy to measure the complex permittivity in the 0.2-2.0 THz range for myoglobin. Both the real and imaginary parts of the permittivity over the frequency range measured have a strong temperature dependence at &amp;gt;0.27 h (g water per g protein), however the permittivity change is strongest for frequencies &amp;lt;1 THz. The temperature dependence of the real part of the permittivity is not consistent with the relaxational response of the bound water, and may reflect the low frequency protein structural vibrations slaved to the solvent excitations. The hydration necessary to observe the dynamical transition is found to be frequency dependent, with a critical hydration of 0.19 h for frequencies &amp;gt;1 THz, and 0.27 h for frequencies &amp;lt;1 THz. The data are consistent with the dynamical transition solvent fluctuations requiring only clusters of similar to 5 water molecules, whereas the enhancement of lowest frequency motions requires a fully spanning water network.&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:000302951500029</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 928AI&lt;br/&gt;Times Cited: 25&lt;br/&gt;Cited Reference Count: 39&lt;br/&gt;Cited References: &lt;br/&gt;     Bonvicini D, 1998, IEEE T DIELECT EL IN, V5, P33, DOI 10.1109/94.660757&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     Brovchenko I, 2008, CHEMPHYSCHEM, V9, P2695, DOI 10.1002/cphc.200800662&lt;br/&gt;     Chen G, 2008, PHILOS MAG, V88, P3877, DOI 10.1080/14786430802585117&lt;br/&gt;     Chen JY, 2005, PHYS REV E, V72, DOI 10.1103/PhysRevE.72.040901&lt;br/&gt;     Chen SH, 2006, P NATL ACAD SCI USA, V103, P9012, DOI 10.1073/pnas.0602474103&lt;br/&gt;     Ding T, 2011, J PHYS CHEM A, V115, P11559, DOI 10.1021/jp200553d&lt;br/&gt;     Doster W, 2010, PHYS REV LETT, V104, DOI 10.1103/PhysRevLett.104.098101&lt;br/&gt;     DOSTER W, 1989, NATURE, V337, P754, DOI 10.1038/337754a0&lt;br/&gt;     Doster W, 2010, BBA-PROTEINS PROTEOM, V1804, P3, DOI 10.1016/j.bbapap.2009.06.019&lt;br/&gt;     Ebbinghaus S, 2007, P NATL ACAD SCI USA, V104, P20749, DOI 10.1073/pnas.0709207104&lt;br/&gt;     Frauenfelder H, 2003, P NATL ACAD SCI USA, V100, P8615, DOI 10.1073/pnas.1633688100&lt;br/&gt;     GASCOYNE PRC, 1977, J CHEM SOC FARAD T 1, V73, P171, DOI 10.1039/f19777300171&lt;br/&gt;     GRISCHKOWSKY D, 1990, J OPT SOC AM B, V7, P2006, DOI 10.1364/JOSAB.7.002006&lt;br/&gt;     HARVEY SC, 1972, J PHYS CHEM-US, V76, P2987, DOI 10.1021/j100665a011&lt;br/&gt;     He YF, 2008, PHYS REV LETT, V101, DOI 10.1103/PhysRevLett.101.178103&lt;br/&gt;     Kauzmann W, 1942, REV MOD PHYS, V14, P0012, DOI 10.1103/RevModPhys.14.12&lt;br/&gt;     Khodadadi S, 2010, BBA-PROTEINS PROTEOM, V1804, P15, DOI 10.1016/j.bbapap.2009.05.006&lt;br/&gt;     Knab J, 2006, BIOPHYS J, V90, P2576, DOI 10.1529/biophysj.105.069088&lt;br/&gt;     Makarov VA, 2000, BIOPHYS J, V79, P2966, DOI 10.1016/S0006-3495(00)76533-7&lt;br/&gt;     Markelz AG, 2008, IEEE J SEL TOP QUANT, V14, P180, DOI 10.1109/JSTQE.2007.913424&lt;br/&gt;     Markelz AG, 2007, CHEM PHYS LETT, V442, P413, DOI 10.1016/j.cplett.2007.05.080&lt;br/&gt;     Oleinikova A, 2005, PHYS REV LETT, V95, DOI 10.1103/PhysRevLett.95.247802&lt;br/&gt;     Oleinikova A, 2005, J PHYS CHEM B, V109, P1988, DOI 10.1021/jp045903j&lt;br/&gt;     Oleinikova A, 2006, MOL PHYS, V104, P3841, DOI 10.1080/00268970601108229&lt;br/&gt;     Paciaroni A, 2008, PHILOS MAG, V88, P4071, DOI 10.1080/14786430802464263&lt;br/&gt;     Parak FG, 2003, CURR OPIN STRUC BIOL, V13, P552, DOI 10.1016/j.sbi.2003.09.004&lt;br/&gt;     Pawlus S, 2008, PHYS REV LETT, V100, DOI 10.1103/PhysRevLett.100.108103&lt;br/&gt;     Roh JH, 2006, BIOPHYS J, V91, P2573, DOI 10.1529/biophysj.106.082214&lt;br/&gt;     Roh JH, 2009, BIOPHYS J, V96, P2755, DOI 10.1016/j.bpj.2008.12.3895&lt;br/&gt;     Roh JH, 2005, PHYS REV LETT, V95, DOI 10.1103/PhysRevLett.95.038101&lt;br/&gt;     RUPLEY JA, 1991, ADV PROTEIN CHEM, V41, P37&lt;br/&gt;     Schiro G, 2011, J PHYS CHEM LETT, V2, P2275, DOI 10.1021/jz200797g&lt;br/&gt;     Shen YC, 2003, APPL PHYS LETT, V82, P2350, DOI 10.1063/1.1565680&lt;br/&gt;     Soderholm S, 2000, J RAMAN SPECTROSC, V31, P995, DOI 10.1002/1097-4555(200011)31:11&lt;995::AID-JRS634&gt;3.0.CO;2-L&lt;br/&gt;     Whitmire SE, 2003, BIOPHYS J, V85, P1269, DOI 10.1016/S0006-3495(03)74562-7&lt;br/&gt;     WU Q, 1995, APPL PHYS LETT, V67, P3523, DOI 10.1063/1.114909&lt;br/&gt;     Zaccai G, 2000, SCIENCE, V288, P1604, DOI 10.1126/science.288.5471.1604&lt;br/&gt;     Zhang CF, 2006, J PHYS CHEM B, V110, P23607, DOI 10.1021/jp063545+&lt;br/&gt;Lipps, Ferdinand Levy, Seth Markelz, A. G.&lt;br/&gt;Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;26&lt;br/&gt;&lt;br/&gt;66&lt;br/&gt;Royal soc chemistry&lt;br/&gt;Cambridge&lt;br/&gt;1463-9084</style></notes><auth-address><style face="normal" font="default" size="100%">[Levy, Seth|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA. [Lipps, Ferdinand] IFW Dresden, Leibniz Inst Solid State &amp; Mat Res, D-01171 Dresden, Germany.&lt;br/&gt;Markelz, AG (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;f.lipps@ifw-dresden.de|sethlevy@buffalo.edu|amarkelz@buffalo.edu</style></auth-address></record></records></xml>