<?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%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Richard, J.</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%">Long Range Correlated Motions of TIM and their Possible Influence on Enzyme Function</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%">2020</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%">118</style></volume><pages><style face="normal" font="default" size="100%">207A-207A</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><abstract><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;The alpha-beta barrel structure of triosephosphate isomerase (TIM) is possibly the most common among enzymes. In the case of TIM, structural dynamics are known to be essential to function. In particular the stabilization of the binding pocket by a phosphodianion “handle” of the substrate and the closing of catalytic site loops 6 and 7 over the substrate. Loop 6 moves by as much as 7 Angstroms with binding. Recently a mutant survey for human TIM (hsTIM) found kcat can change significantly for a single mutation distant from the catalytic site. Crystallographic measurements find no structural change with the mutation, suggesting a dynamical mechanism for the allosteric effect. Here we use Stationary Sample Anisotropic Terahertz Microscopy (SSATM) to measure the long-range intramolecular vibrations and determine if specific vibrations couple the allosteric and catalytic sites. SSATM isolated protein long-range structural vibrations based on the dominant displacement direction [1-4]. We examine if specific vibrational bands are associate with loop 6 and loop 7 flexibility.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000513023201285</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: KK8YX&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.A. M.Y., 2017, BIOPHYS J, DOI [10.1016/j.bpj.2016.12.049.3., DOI 10.1016/J.BPJ.2016.12.049.3]&lt;br/&gt;     Niessen K, 2019, OPT EXPRESS, V27, P28036, DOI 10.1364/OE.27.028036&lt;br/&gt;     Niessen KA, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08926-3&lt;br/&gt;McKinney, Jeffrey A. Deng, Yanting George, Deepu K. Richard, John Markelz, Andrea G.&lt;br/&gt;64th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2020&lt;br/&gt;San Diego, 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]; NIH STTRUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USA [R41 GM125486.1]&lt;br/&gt;This work is supported by NSF grants DBI 1556359 and MCB 1616529, DOE grant DE-SC0016317 and NIH STTR R41 GM125486.1.&lt;br/&gt;&lt;br/&gt;1&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086</style></notes><auth-address><style face="normal" font="default" size="100%">[McKinney, Jeffrey A.|Deng, Yanting|George, Deepu K.|Markelz, Andrea G.] SUNY Buffalo, Univ Buffalo, Phys, Buffalo, NY USA. [Richard, John] SUNY Buffalo, Univ Buffalo, Chem, 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%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</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 Terahertz Microscopy of Protein Collective Vibrations: Crystal Symmetry and Hydration Dependence</style></title><secondary-title><style face="normal" font="default" size="100%">2019 44th 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%">2019</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%">978-1-5386-8285-2</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 stationary sample anisotropic terahertz microscopy technique is used to characterize the intramolecular vibrations for lysozyme. Tetragonal and triclinic crystals are compared. We find excellent reproducibility within a single crystal symmetry group. Several resonant bands are present for both symmetry groups, indicating they originate with the intramolecular vibrations and not crystal lattice phonons. Bands become more pronounced and higher frequency resonant bands begin to emerge with slight dehydration.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000591783800033</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: BQ4OX&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;     Legrand L, 2002, ACTA CRYSTALLOGR D, V58, P1564, DOI 10.1107/S0907444902014403&lt;br/&gt;     Niessen KA, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08926-3&lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;McKinney, Jeffrey Deng, Yanting Sharma, Akansha George, D. K. Markelz, A. G.&lt;br/&gt;Irmmw-thz&lt;br/&gt;Proceedings Paper&lt;br/&gt;44th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)&lt;br/&gt;Sep 01-06, 2019&lt;br/&gt;Paris, FRANCE&lt;br/&gt;Lytid, TYDEX, Swiss Terahertz, Fondat Maison Chimie, CNRS, Lab Physique ENS, Li2S, LUNA, MenloSystems, ENS, PSL Univ Paris, FYLA, ADVANTEST, Springer Nature, Soc Francaise Physique, Sorbonne Univ, Int Soc Infrared Millimeter &amp; Terahertz Waves, IEEE, GDR NANO THz MIR&lt;br/&gt;NSFNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; DOEUnited States Department of Energy (DOE) [DE-SC0016317]; NIHUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USA [STTR R41 GM125486]&lt;br/&gt;This work is supported by NSF grants DBI 1556359 and MCB 1616529, DOE grant DE-SC0016317 and NIH STTR R41 GM125486.&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%">[McKinney, Jeffrey|Deng, Yanting|Sharma, Akansha|George, D. K.|Markelz, A. G.] Univ Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;McKinney, J (corresponding author), 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>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%">McKinney, J.</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%">Deuteration and Inhibitor Binding Dependence of Protein Collective Vibrations</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%">2019</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%">116</style></volume><pages><style face="normal" font="default" size="100%">488A-488A</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:000460779802452</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 2&lt;br/&gt;Cited References: &lt;br/&gt;     Mahajan S, 2015, ARCH BIOCHEM BIOPHYS, V567, P59, DOI 10.1016/j.abb.2014.12.020&lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;Deng, Yanting Mckinney, Jeffrey Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&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|Mckinney, Jeffrey|Markelz, Andrea] SUNY Buffalo, 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%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">George, D.</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%">The Effect of Crystal Contact Forces on the Protein Global Motions</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%">2019</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%">116</style></volume><pages><style face="normal" font="default" size="100%">489A-489A</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:000460779802457</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 1&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;McKinney, Jeffrey A. Deng, Yanting George, Deepu Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&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%">[McKinney, Jeffrey A.|Deng, Yanting|George, Deepu|Markelz, Andrea] Univ Buffalo, 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%">Niessen, K.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</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%">Near-field THz micropolarimetry</style></title><secondary-title><style face="normal" font="default" size="100%">Optics Express</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Opt. Express</style></alt-title><short-title><style face="normal" font="default" size="100%">Opt. ExpressOpt. Express</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">binding</style></keyword><keyword><style  face="normal" font="default" size="100%">conductivity</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">modes</style></keyword><keyword><style  face="normal" font="default" size="100%">Optics</style></keyword><keyword><style  face="normal" font="default" size="100%">polarization modulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Terahertz</style></keyword><keyword><style  face="normal" font="default" size="100%">time-domain spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">wse2</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Sep</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">20</style></number><volume><style face="normal" font="default" size="100%">27</style></volume><pages><style face="normal" font="default" size="100%">28036-28047</style></pages><isbn><style face="normal" font="default" size="100%">1094-4087</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 introduce a method for rapid determination of anisotropic terahertz absorption with sub micron resolution and high spectral integrity in the terahertz range. The method is ideal for microscopic and environmentally sensitive materials such as 2-D materials and protein crystals where the anisotropic absorption is critical to understanding underlying physics. We introduce the idea of using an iso-response relationship between the THz polarization and electro optic probe polarization to enable stationary sample polarization measurements covering a full 2 pi polarization dependence measurement. (C) 2019 Optical Society of America under the terms of the OSA Open Access Publishing Agreement&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:000488282800076</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: JB0XT&lt;br/&gt;Times Cited: 1&lt;br/&gt;Cited Reference Count: 31&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;     Antoniou D, 2011, J PHYS CHEM B, V115, P15147, DOI 10.1021/jp207876k&lt;br/&gt;     Bagsican FR, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-01883-1&lt;br/&gt;     Baxter JB, 2006, J PHYS CHEM B, V110, P25229, DOI 10.1021/jp064399a&lt;br/&gt;     BROOKS B, 1985, P NATL ACAD SCI USA, V82, P4995, DOI 10.1073/pnas.82.15.4995&lt;br/&gt;     Chen JY, 2007, APPL PHYS LETT, V90, DOI 10.1063/1.2748852&lt;br/&gt;     Chhowalla M, 2013, NAT CHEM, V5, P263, DOI [10.1038/NCHEM.1589, 10.1038/nchem.1589]&lt;br/&gt;     Cote Y, 2017, BIOPHYS J, V112, P2575, DOI 10.1016/j.bpj.2017.05.018&lt;br/&gt;     Dhillon SS, 2017, J PHYS D APPL PHYS, V50, DOI 10.1088/1361-6463/50/4/043001&lt;br/&gt;     Docherty CJ, 2014, ACS NANO, V8, P11147, DOI 10.1021/nn5034746&lt;br/&gt;     Ebbinghaus S, 2007, P NATL ACAD SCI USA, V104, P20749, DOI 10.1073/pnas.0709207104&lt;br/&gt;     Fan ST, 2014, J PHYS D APPL PHYS, V47, DOI 10.1088/0022-3727/47/37/374009&lt;br/&gt;     George DK, 2012, J OPT SOC AM B, V29, P1406, DOI 10.1364/JOSAB.29.001406&lt;br/&gt;     GRISCHKOWSKY D, 1990, J OPT SOC AM B, V7, P2006, DOI 10.1364/JOSAB.7.002006&lt;br/&gt;     Hayes D, 2011, FARADAY DISCUSS, V150, P459, DOI 10.1039/c0fd00030b&lt;br/&gt;     Hirota Y, 2006, OPT EXPRESS, V14, P4486, DOI 10.1364/OE.14.004486&lt;br/&gt;     Huang B, 2017, NATURE, V546, P270, DOI 10.1038/nature22391&lt;br/&gt;     Jin WC, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-07547-6&lt;br/&gt;     Lang D, 2018, REV SCI INSTRUM, V89, DOI 10.1063/1.5016281&lt;br/&gt;     Markelz A, 2002, PHYS MED BIOL, V47, P3797, DOI 10.1088/0031-9155/47/21/318&lt;br/&gt;     Meireles L, 2011, PROTEIN SCI, V20, P1645, DOI 10.1002/pro.711&lt;br/&gt;     Niessen KA, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08926-3&lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;     Niessen Katherine A, 2015, Biophys Rev, V7, P201, DOI 10.1007/s12551-015-0168-4&lt;br/&gt;     Ostroverkhova O, 2006, APPL PHYS LETT, V89, DOI 10.1063/1.2387135&lt;br/&gt;     Planken PCM, 2011, J INFRARED MILLIM TE, V32, P975, DOI 10.1007/s10762-011-9824-3&lt;br/&gt;     Planken PCM, 2001, J OPT SOC AM B, V18, P313, DOI 10.1364/JOSAB.18.000313&lt;br/&gt;     Serita K, 2019, PHOTONICS-BASEL, V6, DOI 10.3390/photonics6010012&lt;br/&gt;     Vinh NQ, 2011, J AM CHEM SOC, V133, P8942, DOI 10.1021/ja200566u&lt;br/&gt;     You JW, 2018, NANO CONVERG, V5, DOI 10.1186/s40580-018-0158-x&lt;br/&gt;     Zhao C, 2017, NAT NANOTECHNOL, V12, P757, DOI [10.1038/NNANO.2017.68, 10.1038/nnano.2017.68]&lt;br/&gt;Niessen, Katherine Deng, Yanting Markelz, A. G.&lt;br/&gt;National Science FoundationNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; U.S. Department of EnergyUnited States Department of Energy (DOE) [DE-SCO016317]; National Institute of General Medical SciencesUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [STTR R41 GM125486]&lt;br/&gt;National Science Foundation (DBI 1556359, MCB 1616529); U.S. Department of Energy DE-SCO016317); National Institute of General Medical Sciences (STTR R41 GM125486).&lt;br/&gt;1&lt;br/&gt;3&lt;br/&gt;9&lt;br/&gt;Optical soc amer&lt;br/&gt;Washington</style></notes><auth-address><style face="normal" font="default" size="100%">[Niessen, Katherine|Deng, Yanting|Markelz, A. G.] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Markelz, AG (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;amarkelz@buffatlo.edu</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%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Romo, T.</style></author><author><style face="normal" font="default" size="100%">Grossfield, A.</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%">Spectral Assignment of Lysozyme Collective Vibrations</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%">2019</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%">116</style></volume><pages><style face="normal" font="default" size="100%">564A-564A</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><abstract><style face="normal" font="default" size="100%">&lt;div class=&quot;section-paragraph&quot;&gt;Global structural vibrations at terahertz (THz) frequencies have been associated with protein function and allosteric control. A chief obstacle to utilizing this control mechanism has been measurement of specific motions. Recently it was shown that while the vibrational density of states, and isotropic absorption spectra are broad and featureless, collective vibrations can be isolated based on their directionality using aligned samples (realized with protein crystals) and anisotropic THz microscopy [1]. However the assignment of resonant bands to specific structural motions was complicated by the high symmetry of the tetragonal crystals used, and the slow experimental method. To structurally map the vibrations of the chicken egg white lysozyme (CEWL) we measure anisotropic absorption of triclinic crystals using our new technique: ideal polarization varying anisotropic THz microscopy (IPV-ATM). The low symmetry triclinic crystals provide absolute protein orientation, and the near field IPV-ATM rapidly measures broadband terahertz linear dichroism of the microcrystals. All measurements were performed at room temperature under 100% humidity conditions. The unit cell parameters of triclinic lysozyme nitrate crystals, α = 28.5A°, b = 32.7A°, c = 35.1A°, α = 88.2°, β = 108.9°, γ = 111.9°, belonging to the P1 space group, were determined by X-ray diffraction before and after THz measurements. The intramolecular vibrational absorbance of the triclinic crystals has a more complex polarization dependence than the higher symmetry tetragonal crystals, as expected. While the tetragonal crystals have two strong bands at 45cm&lt;sup&gt;−1&lt;/sup&gt; and 55cm&lt;sup&gt;−1&lt;/sup&gt;, the triclinic crystals have a series of narrow bands between 40 and 60cm&lt;sup&gt;−1&lt;/sup&gt; and a prominent band at 30cm&lt;sup&gt;−1&lt;/sup&gt;. We compare the measured spectra to normal mode ensemble averaged calculations to assign the observed resonances, and isolating which collective motions impact the catalytic site.&lt;/div&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000460779802832</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 1&lt;br/&gt;Cited References: &lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;Deng, Yanting Mckinney, Jeffrey Romo, Tod Grossfield, Alan Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&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|Mckinney, Jeffrey|Markelz, Andrea] SUNY Buffalo, Phys, Buffalo, NY USA. [Romo, Tod|Grossfield, Alan] Univ Rochester, Med Ctr, Dept Biochem &amp; Biophys, Rochester, NY 14642 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%">Luck, C. H.</style></author><author><style face="normal" font="default" size="100%">Romo, T. D.</style></author><author><style face="normal" font="default" size="100%">Grossfield, A. M.</style></author><author><style face="normal" font="default" size="100%">Bandara, S.</style></author><author><style face="normal" font="default" size="100%">Ren, Z.</style></author><author><style face="normal" font="default" size="100%">Yang, X. J.</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%">Increase in Dynamical Collectivity and Directionality of Orange Carotenoid Protein in the Photo-Protective State</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%">2018</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%">114</style></volume><pages><style face="normal" font="default" size="100%">522A-522A</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:000430563200362</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: GD5RB&lt;br/&gt;Times Cited: 1&lt;br/&gt;Cited Reference Count: 0&lt;br/&gt;Deng, Yanting Luck, Catherine H. Romo, Tod D. Grossfield, Alan M. Bandara, Sepalika Ren, Zhong Yang, Xiaojing Markelz, Andrea G.&lt;br/&gt;62nd Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 17-21, 2018&lt;br/&gt;San Francisco, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;1&lt;br/&gt;&lt;br/&gt;7&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Luck, Catherine H.|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Romo, Tod D.|Grossfield, Alan M.] Univ Rochester, Med Ctr, Dept Biochem &amp; Biophys, Rochester, NY 14642 USA. [Bandara, Sepalika|Ren, Zhong|Yang, Xiaojing] Univ Illinois, Dept Chem, Chicago, IL 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%">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></records></xml>