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Protein Science (2007), 16:2317-2333. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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REVIEW

Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency

Jannette Carey1, Stina Lindman2, Mikael Bauer2, and Sara Linse2

1 Chemistry Department, Princeton University, Princeton, New Jersey, 08544-1009 USA
2 Department of Biophysical Chemistry, Chemical Center, Lund University, S22100 Lund, Sweden

(RECEIVED May 4, 2007; FINAL REVISION July 30, 2007; ACCEPTED August 1, 2007)

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: stability; metastability; steric constraints; cooperativity; ligand binding


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