A reduced model of short range interactions in polypeptide chains

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Author(s)
Kolinski, Andrzej
Milik, Mariusz
Rycombel, Jakub
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School of Biological Sciences
School established in 2016 with the merger of the Schools of Applied Physiology and Biology
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Abstract
A simple model of short range interactions is proposed for a reduced lattice representation of polypeptide conformation. The potential is derived on the basis of statistical regularities seen in the known crystal structures of globular proteins. This potential accounts for the generic stiffness of polypeptides, the correlation between peptide bond plates, and the sequence dependent correlations between consecutive segments of the C-trace. This model is used for simulation of the equilibrium and dynamic properties of polypeptides in the denatured state. It is shown that the proposed factorization of the local conformational propensities reproduces secondary structure tendencies encoded in the protein sequence. Possible applications for modeling of protein folding are briefly discussed.
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1995-09-08
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