Abstract
A review of physical regularities in formation of the the spatial structure of proteins during their folding, that is, the folding of a homochiral polypeptide chain into a unique native configuration, is presented, including the mathematical models of this process. The materials of this review are summarized in a new phenomenological model for the formation of hierarchies of sign-alternating chiral structures and also in a new mathematical model for the formation of α-helices as autowave structures. Some folding thermodynamic aspects associated with symmetry factors are discussed.
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