Protein Reconstitution and Three-dimensional Domain Swapping: Benefits and Constraints of Covalency

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2007 Oct 27

PMID 17962398

Citations 24

Authors

Jannette Carey

Stina Lindman

Mikael Bauer

Sara Linse

Affiliations

Soon will be listed here.

Abstract

The phenomena of protein reconstitution and three-dimensional domain swapping reveal that highly similar structures can be obtained whether a protein is comprised of one or more polypeptide chains. In this review, we use protein reconstitution as a lens through which to examine the range of protein tolerance to chain interruptions and the roles of the primary structure in related features of protein structure and folding, including circular permutation, natively unfolded proteins, allostery, and amyloid fibril formation. The results imply that noncovalent interactions in a protein are sufficient to specify its structure under the constraints imposed by the covalent backbone.

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