期刊
PHYSICAL REVIEW LETTERS
卷 85, 期 1, 页码 206-209出版社
AMERICAN PHYSICAL SOC
DOI: 10.1103/PhysRevLett.85.206
关键词
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Since it is not feasible to determine the structure of every protein by experiment, algorithms delivering the folded conformation of a protein solely from its amino acid sequence are desirable. Here the diffusion-process controlled-Monte Carlo approach has been applied to generating ensemble averages for three small proteins with 31, 36, and 46 residues. Starting from extended conformations and using an energy model that was developed on other protein models, the simulations find nativelike structures deviating by 3 Angstrom rms from the experimental structures for the main chain atoms. The balance between long-range and short-range interactions is discussed briefly in the context of stability and folding.
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