000080933 001__ 80933
000080933 005__ 20180317094758.0
000080933 037__ $$aARTICLE
000080933 245__ $$aProtein dynamics, thermal stability, and free-energy landscapes: A molecular dynamics investigation
000080933 269__ $$a2003
000080933 260__ $$c2003
000080933 336__ $$aJournal Articles
000080933 520__ $$aProteins have a complex free-energy landscape because of their rich topol. and the nature of their nonbonded interaction potential. This has important consequences because the roughness of the landscape affects the ease with which a chain folds and also dets. the dynamic behavior of the folded structure, thus influencing its functional and stability properties. A detailed description of the free-energy landscape is therefore of paramount importance for a quant. understanding of the relationships between structure, dynamics, stability, and functional behavior of proteins. The free-energy landscape of a protein is a high-dimensional hypersurface, difficult to rationalize. Therefore, achieving its detailed graphical representation in a way that goes beyond the familiar funnel-like free-energy model is still a big challenge. We describe here an approach based on global structural parameters that allows a two-dimensional representation of the free-energy landscape from simulated at. trajectories. As shown in this and in the accompanying article, our representation of the landscape, combined with other conformational analyses, provides valuable information on its roughness and on how at. trajectories evolve with time. [on SciFinder (R)]
000080933 700__ $$0240258$$aTavernelli, Ivano$$g153498
000080933 700__ $$aCotesta, Simona
000080933 700__ $$aDi Iorio, Ernesto E.
000080933 773__ $$j85$$k4$$q2641-2649$$tBiophysical Journal
000080933 909CO $$ooai:infoscience.tind.io:80933$$particle$$pSB
000080933 909C0 $$0252093$$pLCBC$$xU2
000080933 937__ $$aLCBC-ARTICLE-2003-006
000080933 970__ $$a137/LCBC
000080933 973__ $$aEPFL$$rREVIEWED$$sPUBLISHED
000080933 980__ $$aARTICLE