Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency. Author Jannette Carey, Stina Lindman, Mikael Bauer, Sara Linse 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 Animals, Humans, Protein Binding, Models, Molecular, Ligands, Protein Structure, Tertiary, Protein Conformation, Kinetics, Amino Acid Sequence, Protein Folding, Entropy, Proteins, Molecular Conformation, Models, Chemical Journal Protein Sci Volume 16 Issue 11 Pages 2317-33 Date Published 2007 Nov ISSN Number 0961-8368 DOI 10.1110/ps.072985007 Alternate Journal Protein Sci PMCID PMC2211703 PMID 17962398 PubMedPubMed CentralGoogle ScholarBibTeXEndNote X3 XML