<?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%">Whitmire, S. E.</style></author><author><style face="normal" font="default" size="100%">Wolpert, D.</style></author><author><style face="normal" font="default" size="100%">Markelz, A. G.</style></author><author><style face="normal" font="default" size="100%">Hillebrecht, J. R.</style></author><author><style face="normal" font="default" size="100%">Galan, J.</style></author><author><style face="normal" font="default" size="100%">Birge, R. R.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protein flexibility and conformational state: A comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsin</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%">angstrom resolution</style></keyword><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword><keyword><style  face="normal" font="default" size="100%">dna</style></keyword><keyword><style  face="normal" font="default" size="100%">films</style></keyword><keyword><style  face="normal" font="default" size="100%">frequency</style></keyword><keyword><style  face="normal" font="default" size="100%">harmonic-analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">inelastic neutron-scattering</style></keyword><keyword><style  face="normal" font="default" size="100%">large systems</style></keyword><keyword><style  face="normal" font="default" size="100%">mixed basis</style></keyword><keyword><style  face="normal" font="default" size="100%">normal-modes</style></keyword><keyword><style  face="normal" font="default" size="100%">purple membranes</style></keyword><keyword><style  face="normal" font="default" size="100%">structural-changes</style></keyword><keyword><style  face="normal" font="default" size="100%">transform infrared-spectroscopy</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Aug</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><volume><style face="normal" font="default" size="100%">85</style></volume><pages><style face="normal" font="default" size="100%">1269-1277</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&gt;Far infrared ( FIR) spectral measurements of wild-type (WT) and D96N mutant bacteriorhodopsin thin films have been carried out using terahertz time domain spectroscopy as a function of hydration, temperature, and conformational state. The results are compared to calculated spectra generated via normal mode analyses using CHARMM. We find that the FIR absorbance is slowly increasing with frequency and without strong narrow features over the range of 2-60 cm(-1) and up to a resolution of 0.17 cm(-1). The broad absorption shifts in frequency with decreasing temperature as expected with a strongly anharmonic potential and in agreement with neutron inelastic scattering results. Decreasing hydration shifts the absorption to higher frequencies, possibly resulting from decreased coupling mediated by the interior water molecules. Ground-state FIR absorbances have nearly identical frequency dependence, with the mutant having less optical density than the WT. In the M state, the FIR absorbance of the WT increases whereas there is no change for D96N. These results represent the first measurement of FIR absorbance change as a function of conformational state.&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:000184428300052</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 705ZZ&lt;br/&gt;Times Cited: 117&lt;br/&gt;Cited Reference Count: 55&lt;br/&gt;Cited References: &lt;br/&gt;     AUSTIN RH, 1975, BIOCHEMISTRY-US, V14, P5355, DOI 10.1021/bi00695a021&lt;br/&gt;     Birge RR, 1996, J PHYS CHEM-US, V100, P9990, DOI 10.1021/jp953669e&lt;br/&gt;     BOUSCHE O, 1992, PHOTOCHEM PHOTOBIOL, V56, P1085, DOI 10.1111/j.1751-1097.1992.tb09732.x&lt;br/&gt;     BROOKS BR, 1983, J COMPUT CHEM, V4, P187, DOI 10.1002/jcc.540040211&lt;br/&gt;     BROOKS BR, 1995, J COMPUT CHEM, V16, P1522, DOI 10.1002/jcc.540161209&lt;br/&gt;     Brooks CL, 1988, PROTEINS THEORETICAL&lt;br/&gt;     Brucherseifer M, 2000, APPL PHYS LETT, V77, P4049, DOI 10.1063/1.1332415&lt;br/&gt;     Chen Q, 2001, J OPT SOC AM B, V18, P823, DOI 10.1364/JOSAB.18.000823&lt;br/&gt;     DENCHER NA, 1989, P NATL ACAD SCI USA, V86, P7876, DOI 10.1073/pnas.86.20.7876&lt;br/&gt;     Der A, 2001, BIOCHEMISTRY-MOSCOW+, V66, P1234, DOI 10.1023/A:1013179101782&lt;br/&gt;     Diehl M, 1997, BIOPHYS J, V73, P2726, DOI 10.1016/S0006-3495(97)78301-2&lt;br/&gt;     DOSTER W, 1989, NATURE, V337, P754, DOI 10.1038/337754a0&lt;br/&gt;     FERRAND M, 1993, P NATL ACAD SCI USA, V90, P9668, DOI 10.1073/pnas.90.20.9668&lt;br/&gt;     GENZEL L, 1984, SPECTROSCOPY BIOL MO, P609&lt;br/&gt;     GRISCHKOWSKY D, 1991, OSA PROC, V9, P9&lt;br/&gt;     Guilbert C, 1996, CHEM PHYS, V204, P327, DOI 10.1016/0301-0104(95)00293-6&lt;br/&gt;     Han PY, 2000, OPT LETT, V25, P242, DOI 10.1364/OL.25.000242&lt;br/&gt;     Hinsen K, 1998, PROTEINS, V33, P417, DOI 10.1002/(SICI)1097-0134(19981115)33:3&lt;417::AID-PROT10&gt;3.0.CO;2-8&lt;br/&gt;     JANEZIC D, 1995, J COMPUT CHEM, V16, P1543, DOI 10.1002/jcc.540161210&lt;br/&gt;     Kusnetzow A, 1999, BIOPHYS J, V76, P2370, DOI 10.1016/S0006-3495(99)77394-7&lt;br/&gt;     Lanyi JK, 1999, INT REV CYTOL, V187, P161, DOI 10.1016/S0074-7696(08)62418-3&lt;br/&gt;     Lanyi JK, 2001, TRENDS BIOTECHNOL, V19, P140, DOI 10.1016/S0167-7799(01)01576-1&lt;br/&gt;     LINDSAY SM, 1988, BIOPOLYMERS, V27, P1015, DOI 10.1002/bip.360270610&lt;br/&gt;     Lisy V, 1997, J BIOMOL STRUCT DYN, V14, P517, DOI 10.1080/07391102.1997.10508150&lt;br/&gt;     LONGBOTTOM C, 2002, POTENTIAL USES TERAH&lt;br/&gt;     Luecke H, 1999, SCIENCE, V286, P255, DOI 10.1126/science.286.5438.255&lt;br/&gt;     Luecke H, 1999, J MOL BIOL, V291, P899, DOI 10.1006/jmbi.1999.3027&lt;br/&gt;     MacKerell AD, 1998, J PHYS CHEM B, V102, P3586, DOI 10.1021/jp973084f&lt;br/&gt;     Markelz AG, 2000, CHEM PHYS LETT, V320, P42, DOI 10.1016/S0009-2614(00)00227-X&lt;br/&gt;     MCINTOSH AR, 1991, BIOPHYS J, V60, P1, DOI 10.1016/S0006-3495(91)82025-2&lt;br/&gt;     MOUAWAD L, 1993, BIOPOLYMERS, V33, P599, DOI 10.1002/bip.360330409&lt;br/&gt;     Mouawad L, 1996, J MOL BIOL, V258, P393, DOI 10.1006/jmbi.1996.0257&lt;br/&gt;     Nagel M, 2002, APPL PHYS LETT, V80, P154, DOI 10.1063/1.1428619&lt;br/&gt;     Oesterhelt D, 1974, Methods Enzymol, V31, P667&lt;br/&gt;     Palmo K, 1998, J COMPUT CHEM, V19, P754, DOI 10.1002/(SICI)1096-987X(199805)19:7&lt;754::AID-JCC6&gt;3.0.CO;2-P&lt;br/&gt;     PERAHIA D, 1995, COMPUT CHEM, V19, P241, DOI 10.1016/0097-8485(95)00011-G&lt;br/&gt;     Person W.B., 1982, VIBRATIONAL INTENSIT&lt;br/&gt;     Polavarapu P. 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Univ Connecticut, Dept Chem, Storrs, CT USA. Univ Connecticut, Dept Mol &amp; Cell Biol, Storrs, CT 06269 USA.&lt;br/&gt;Markelz, AG (corresponding author), SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;amarkelz@buffalo.edu</style></auth-address></record></records></xml>