Recent developments in the theory of protein folding: searching for the global energy minimum.
Statistical mechanical theories and computer simulation are being used to gain an understanding of the fundamental features of protein folding. A major obstacle in the computation of protein structures is the multiple-minima problem arising from the existence of many local minima in the multidimensional energy landscape of the protein. This problem has been surmounted for small open-chain and cyclic peptides, and for regular-repeating sequences of models of fibrous proteins. Progress is being made in resolving this problem for globular proteins.
Scheraga
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Baker Laboratory of Chemistry, Cornell University, Ithaca, NY 14853-1301, USA.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D015233:Models, Statistical; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins