Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.
Publication Year
2007
Type
Journal Article
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.
Keywords
Journal
Protein Sci
Volume
16
Issue
11
Pages
2317-33
Date Published
2007 Nov
ISSN Number
0961-8368
Alternate Journal
Protein Sci
PMCID
PMC2211703
PMID
17962398