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pubmed-article:11913387pubmed:abstractTextThe evolution of our physics-based computational methods for determining protein conformation without the introduction of secondary-structure predictions, homology modeling, threading, or fragment coupling is described. Initial use of a hard-sphere potential captured much of the structural properties of polypeptide chains, and subsequent more refined force fields, together with efficient methods of global optimization provide indications that progress is being made toward an understanding of the interresidue interactions that underlie protein folding.lld:pubmed
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pubmed-article:11913387pubmed:pagination28-34lld:pubmed
pubmed-article:11913387pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:11913387pubmed:articleTitleEvolution of physics-based methodology for exploring the conformational energy landscape of proteins.lld:pubmed
pubmed-article:11913387pubmed:affiliationBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA. has5@cornell.edulld:pubmed
pubmed-article:11913387pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11913387pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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