Search for the most stable folds of protein chains: I. Application of a self-consistent molecular field theory to a problem of protein three-dimensional structure prediction

We present a general approach to the prediction of 3-D folds of protein chains from their amino acid sequences. The approach is based on the use of the self-consistent molecular field theory for long-range interactions, the use of 1-D statistical mechanics for short-range interactions and on the dis...

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Bibliographic Details
Published in:Protein engineering 1996-05, Vol.9 (5), p.387-397
Main Authors: Finkelstein, A V, Reva, B A
Format: Article
Language:English
Subjects:
Models, Molecular
Protein Structure, Tertiary
Online Access:Get full text
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Summary:We present a general approach to the prediction of 3-D folds of protein chains from their amino acid sequences. The approach is based on the use of the self-consistent molecular field theory for long-range interactions, the use of 1-D statistical mechanics for short-range interactions and on the discovery that there is and should only be a relatively small discrete set of folding patterns. This makes it possible to examine the full variety of 'potentially stable' folds and to determine the thermodynamically stable structure. In this paper, we give the general theoretical background of the approach. The encouraging results of the application of this approach to beta-domains are described in another paper.
ISSN:0269-2139