SEARCH FOR THE MOST STABLE FOLDS OF PROTEIN CHAINS .2. COMPUTATION OFSTABLE ARCHITECTURES OF BETA-PROTEINS USING A SELF-CONSISTENT MOLECULAR-FIELD THEORY

In a preceding paper we presented a novel approach to computation of 3 -D folds of protein chains from their amino acid sequences. This appro ach is a physically correct generalization of the 'threading' methods. It is based on a self-consistent molecular field theory and on a phys ical theory of protein folding patterns, which make it possible to exa mine all the variety of 'potentially stable' folding patterns and all the variety of the chain conformations within each of them and to dete rmine the thermodynamically stable structure. In this paper, we apply this approach to single out stable folding patterns and conformations for the chains of beta-sandwich proteins and show that the similarity of the calculated and observed structures is usually rather close.