<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Haspel, N.</style></author><author><style face="normal" font="default" size="100%">Moll, Mark</style></author><author><style face="normal" font="default" size="100%">Baker, M. L.</style></author><author><style face="normal" font="default" size="100%">Chiu, W.</style></author><author><style face="normal" font="default" size="100%">L. E. Kavraki</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Tracing Conformational Changes in Proteins</style></title><secondary-title><style face="normal" font="default" size="100%">IEEE Intl. Conf. on Bioinformatics and Biomedicine Workshops (BIBMW)</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">kavrakilab</style></keyword><keyword><style  face="normal" font="default" size="100%">protein motion</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year></dates><pub-location><style face="normal" font="default" size="100%">Washington, DC</style></pub-location><abstract><style face="normal" font="default" size="100%">Many proteins undergo extensive conformational changes as part of their functionality. Tracing these changes is important for understanding the way these proteins function. Traditional biophysics-based conformational search methods re- quire a large number of calculations and are hard to apply to large-scale conformational motions. In this work we investigate the application of a robotics-inspired method, using backbone and limited side chain representation and a coarse grained energy function to trace large-scale conformational motions. We tested the algorithm on three well known medium to large proteins and we show that even with relatively little information we are able to trace low-energy conformational pathways efficiently. The conformational pathways produced by our methods can be further filtered and refined to produce more useful information on the way proteins function under physiological conditions.</style></abstract></record></records></xml>
