<?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%">Wang, Jianping</style></author><author><style face="normal" font="default" size="100%">El-Sayed, Mostafa A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Temperature jump-induced secondary structural change of the membrane protein bacteriorhodopsin in the premelting temperature region: A nanosecond time-resolved Fourier transform infrared study</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">May</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5</style></number><volume><style face="normal" font="default" size="100%">76</style></volume><pages><style face="normal" font="default" size="100%">2777-2783</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The secondary structural changes of the membrane protein, bacteriorhodopsin, are studied during the premelting reversible transition by using laser-induced temperature jump technique and nanosecond time-resolved Fourier transform infrared spectroscopy. The helical structural changes are triggered by using a 15 degrees C temperature jump induced from a preheated bacteriorhodopsin in D2O solution at a temperature of 72 degrees C. The structural transition from alpha(II)- to alpha(I)-helices is observed by following the change in the frequency of the amide I band from 1667 to 1651 cm(-1) and the shift in the frequency of the amide II vibration from 1542 cm(-1) to 1436 cm(-1) upon H/D exchange. It is found that although the amide I band changes its frequency on a time scale of &lt;100 ns, the H/D exchange shifts the frequency of the amide II band and causes a complex changes in the 1651-1600 cm(-1) and 1530-1430 cm(-1) frequency region on a longer time scale (&gt;300 ns). Our result suggests that in this &quot;premelting transition&quot; temperature region of bacterioriorhodopsin, an intrahelical conformation conversion of the alpha(II) to alpha(I) leads to the exposure of the hydrophobic region of the protein to the aqueous medium.</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000080278600043</style></accession-num><notes><style face="normal" font="default" size="100%">Wang, JP El-Sayed, MA</style></notes></record></records></xml>