<?xml version="1.0" encoding="UTF-8"?><xml><records><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%">Niessen, K. A.</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%">Measurements and Calculations of Protein Intramolecular Vibrations in the THz Range</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%">charmm</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;We report the calculations and measurements of intramolecular vibrational modes and their dependence on inhibitor binding in the THz range. We see an increase in anisotropic THz absorption at low frequency with inhibitor binding in both the measurements and calculations. This surprising result suggests an increase in flexibility with binding. We will discuss the possible reasons for this discrepancy.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000378889200091</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: 13&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Balog E, 2004, PHYS REV LETT, V93, DOI 10.1103/PhysRevLett.93.028103&lt;br/&gt;     Best RB, 2012, J CHEM THEORY COMPUT, V8, P3257, DOI 10.1021/ct300400x&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     BRUCCOLERI RE, 1986, BIOPOLYMERS, V25, P1767, DOI 10.1002/bip.360250916&lt;br/&gt;     CHEETHAM JC, 1992, J MOL BIOL, V224, P613, DOI 10.1016/0022-2836(92)90548-X&lt;br/&gt;     Dong J, 1999, ACTA CRYSTALLOGR D, V55, P745, DOI 10.1107/S0907444998016047&lt;br/&gt;     Guo JN, 2014, BIOCHEMISTRY-US, V53, P2855, DOI 10.1021/bi500238q&lt;br/&gt;     Hammes-Schiffer S, 2006, ANNU REV BIOCHEM, V75, P519, DOI 10.1146/annurev.biochem.75.103004.142800&lt;br/&gt;     Henzler-Wildman KA, 2007, NATURE, V450, P838, DOI 10.1038/nature06410&lt;br/&gt;     Jo S, 2008, J COMPUT CHEM, V29, P1859, DOI 10.1002/jcc.20945&lt;br/&gt;     PERUTZ MF, 1970, NATURE, V228, P726, DOI 10.1038/228726a0&lt;br/&gt;     TEETER MM, 1990, J PHYS CHEM-US, V94, P8091, DOI 10.1021/j100384a021&lt;br/&gt;Niessen, Katherine A. Snell, Edward 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;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%">[Niessen, Katherine A.|Markelz, A. G.] SUNY Buffalo, Univ Buffalo, Dept Phys, Buffalo, NY 14260 USA. [Snell, Edward|Markelz, A. G.] SUNY Buffalo, Univ Buffalo, Hauptman Woodward Med Res Inst, Buffalo, NY 14203 USA. [Snell, Edward|Markelz, A. G.] SUNY Buffalo, Univ Buffalo, Dept Biol Struct, Buffalo, NY 14203 USA.&lt;br/&gt;Niessen, KA (corresponding author), SUNY Buffalo, Univ Buffalo, Dept Phys, Buffalo, NY 14260 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%">Acbas, G.</style></author><author><style face="normal" font="default" size="100%">Niessen, K. A.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</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><secondary-authors><author><style face="normal" font="default" size="100%">Betz, M.</style></author><author><style face="normal" font="default" size="100%">Elezzabi, A. Y.</style></author><author><style face="normal" font="default" size="100%">Song, J. J.</style></author><author><style face="normal" font="default" size="100%">Tsen, K. T.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">Measuring phonons in protein crystals</style></title><secondary-title><style face="normal" font="default" size="100%">Ultrafast Phenomena and Nanophotonics Xvii</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%">correlated motions</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">mode</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular crystals</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular vibrations</style></keyword><keyword><style  face="normal" font="default" size="100%">normal modes</style></keyword><keyword><style  face="normal" font="default" size="100%">phonons</style></keyword><keyword><style  face="normal" font="default" size="100%">protein dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Terahertz</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</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%">8623</style></volume><isbn><style face="normal" font="default" size="100%">978-0-8194-9392-7</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Using Terahertz near field microscopy we find orientation dependent narrow band absorption features for lysozyme crystals. Here we discuss identification of protein collective modes associated with the observed features. Using normal mode calculations we find good agreement with several of the measured features, suggesting that the modes arise from internal molecular motions and not crystal phonons. Such internal modes have been associated with protein function.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000322829300003</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BGG42&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 5&lt;br/&gt;Cited References: &lt;br/&gt;     Bahar I, 2005, CURR OPIN STRUC BIOL, V15, P586, DOI 10.1016/j.sbi.2005.08.007&lt;br/&gt;     BROOKS B, 1985, P NATL ACAD SCI USA, V82, P4995, DOI 10.1073/pnas.82.15.4995&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     Karplus M, 2005, P NATL ACAD SCI USA, V102, P6679, DOI 10.1073/pnas.0408930102&lt;br/&gt;     Planken PCM, 2011, J INFRARED MILLIM TE, V32, P975, DOI 10.1007/s10762-011-9824-3&lt;br/&gt;Acbas, Gheorghe Niessen, Katherine A. George, Deepu K. Snell, Edward Markelz, A. G.&lt;br/&gt;Proceedings Paper&lt;br/&gt;Conference on Ultrafast Phenomena and Nanophotonics XVII&lt;br/&gt;Feb 03-06, 2013&lt;br/&gt;San Francisco, CA&lt;br/&gt;SPIE, Femtolasers Inc&lt;br/&gt;Snell, Edward/G-2055-2018; George, Deepu/J-9882-2014&lt;br/&gt;Snell, Edward/0000-0001-8714-3191; George, Deepu/0000-0003-0021-0705; Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;National Science Foundation MRI2 [DBI2959989]&lt;br/&gt;We thank the National Science Foundation MRI2 grant DBI2959989 for support.&lt;br/&gt;1000 20th st, po box 10, bellingham, wa 98227-0010 usa&lt;br/&gt;0277-786x&lt;br/&gt;862305</style></notes><auth-address><style face="normal" font="default" size="100%">[Acbas, Gheorghe|Niessen, Katherine A.|George, Deepu K.|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA. [Snell, Edward] SUNY Buffalo, Dept Struct Biol, Buffalo, NY 14260 USA.&lt;br/&gt;Acbas, G (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 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%">Acbas, G.</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%">Orientation Sensitive Terahertz Resonances Observed in Protein Crystals</style></title><secondary-title><style face="normal" font="default" size="100%">2012 37th 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><keyword><style  face="normal" font="default" size="100%">mode</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</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%">978-1-4673-1597-5</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A method is presented for measuring anisotropic THz response for small crystals, Crystal Anisotropy Terahertz Microscopy (CATM). Sucrose CATM measurements find the expected anisotropic phonon resonances. CATM measurements of protein crystals find the expected broadband water absorption is suppressed and strong orientation and hydration dependent resonant features.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000330301800120</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BJT74&lt;br/&gt;Times Cited: 1&lt;br/&gt;Cited Reference Count: 15&lt;br/&gt;Cited References: &lt;br/&gt;     Arora K, 2007, P NATL ACAD SCI USA, V104, P18496, DOI 10.1073/pnas.0706443104&lt;br/&gt;     Bahar I, 2005, CURR OPIN STRUC BIOL, V15, P586, DOI 10.1016/j.sbi.2005.08.007&lt;br/&gt;     Balu R, 2008, BIOPHYS J, V94, P3217, DOI 10.1529/biophysj.107.105163&lt;br/&gt;     BROOKS B, 1985, P NATL ACAD SCI USA, V82, P4995, DOI 10.1073/pnas.82.15.4995&lt;br/&gt;     Goodey NM, 2008, NAT CHEM BIOL, V4, P474, DOI 10.1038/nchembio.98&lt;br/&gt;     Hammes-Schiffer S, 2006, ANNU REV BIOCHEM, V75, P519, DOI 10.1146/annurev.biochem.75.103004.142800&lt;br/&gt;     Jarymowycz VA, 2006, CHEM REV, V106, P1624, DOI 10.1021/cr040421p&lt;br/&gt;     Karplus M, 2005, P NATL ACAD SCI USA, V102, P6679, DOI 10.1073/pnas.0408930102&lt;br/&gt;     Knab JR, 2010, APPL PHYS LETT, V97, DOI 10.1063/1.3467192&lt;br/&gt;     Lange OF, 2008, SCIENCE, V320, P1471, DOI 10.1126/science.1157092&lt;br/&gt;     Liu D, 2008, PHYS REV LETT, V101, DOI 10.1103/PhysRevLett.101.135501&lt;br/&gt;     Mellinger JS, 2007, J PHYS CHEM A, V111, P10977, DOI 10.1021/jp074975i&lt;br/&gt;     Planken PCM, 2011, J INFRARED MILLIM TE, V32, P975, DOI 10.1007/s10762-011-9824-3&lt;br/&gt;     Rheinstadter MC, 2009, PHYS REV LETT, V103, DOI 10.1103/PhysRevLett.103.128104&lt;br/&gt;     Tych KM, 2011, J APPL CRYSTALLOGR, V44, P129, DOI 10.1107/S0021889810043372&lt;br/&gt;Acbas, Gheorghe Snell, Edward Markelz, A. G.&lt;br/&gt;Irmmw-thz&lt;br/&gt;Proceedings Paper&lt;br/&gt;37th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)&lt;br/&gt;Sep 23-28, 2012&lt;br/&gt;Univ Wollongong, Wollongong, AUSTRALIA&lt;br/&gt;IEEE, USN, Off Naval Res Sci &amp; Technol, ETRI, UOW, Sch Engn Phys, Ctr Ultrahigh Bandwidth Devices Opt Syst, Victoria Suntech Adv Solar Facil, Swinburne, Ctr Micro Photon, Edinburgh Photon, Tydex, TRAS Inc, Inst Photon &amp; Opt Sci, LakeShore, Australian Synchrotron, CSIRO, Univ Wollongong, Inst Superconducting &amp; Elect Mat, Ctr Med Radiat Phys, Univ Sydney, IEEE Microwave Theory &amp; Tech Soc&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%">[Acbas, Gheorghe|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Acbas, G (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;amarkelz@buffalo.edu</style></auth-address></record></records></xml>