SEARCH FOR THE MOST STABLE FOLDS OF PROTEIN CHAINS .1. APPLICATION OFA SELF-CONSISTENT MOLECULAR HELD THEORY TO A PROBLEM OF PROTEIN 3-DIMENSIONAL STRUCTURE PREDICTION

We present a general approach to the prediction of 3-D folds of protei n chains from their amino acid sequences. The approach is based on the use of the self-consistent molecular held theory for long-range inter actions, the use of 1-D statistical mechanics for short-range interact ions and on the discovery that there is and should only be a relativel y small discrete set of folding patterns, This makes it possible to ex amine the full variety of 'potentially stable' folds and to determine the thermodynamically stable structure. In this paper, we give the gen eral theoretical background of the approach, The encouraging results o f the application of this approach to beta-domains are described in an other paper.