Recursive domains in proteins.

Teresa Przytycka; Rajgopal Srinivasan; George D Rose

doi:10.1110/ps.24701

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Recursive domains in proteins.

Teresa Przytycka·Rajgopal Srinivasan·George D Rose

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Abstract

The domain is a fundamental unit of protein structure. Numerous studies have analyzed folding patterns in protein domains of known structure to gain insight into the underlying protein folding process. Are such patterns a haphazard assortment or are they similar to sentences in a language, which can be generated by an underlying grammar? Specifically, can a small number of intuitively sensible rules generate a large class of folds, including feasible new folds? In this paper, we explore the extent to which four simple rules can generate the known all-beta folds, using tools from graph theory. As a control, an exhaustive set of beta-sandwiches was tested and found to be largely incompatible with such a grammar. The existence of a protein grammar has potential implications for both the mechanism of folding and the evolution of domains.

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Dimerization Kinetics Models, Molecular Protein Conformation Protein Folding Protein Structure, Tertiary Proteins Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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Teresa Przytycka, Rajgopal Srinivasan, George D Rose. 2002. Recursive domains in proteins.. https://doi.org/10.1110/ps.24701

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