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 foldsof protein chains from their amino acid sequences. The approachis based on the use of the self-consistent molecular field theoryfor long-range interactions, the use of 1-D statistical mechanicsfor short-range interactions and on the discovery that thereis and should only be a relatively small discrete set of foldingpatterns. This makes it possible to examine the full varietyof ‘potentially stable’ folds and to determine thethermodynamically stable structure. In this paper, we give thegeneral theoretical background of the approach. The encouragingresults of the application of this approach to ß-domainsare described in another paper.