[Determination of the folding of globular protein chain by the self-consistent field method].

It is shown that and how it is possible to single out the chain fold which is thermo-dynamically most stable. The suggested approach is based on two physical ideas: A "molecular field" approximation permits to examine all protein structures which belong to the same "folding pattern". Only a limited set of the "potentially stable" folding patterns have to be examined. The general approach is illustrated by calculations of the stable folds for two beta-domains.