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

TitleProtein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.
Publication TypeJournal Article
Year of Publication2007
AuthorsCarey, J, Lindman, S, Bauer, M, Linse, S
JournalProtein Sci
Volume16
Issue11
Pagination2317-33
Date Published2007 Nov
ISSN0961-8368
KeywordsAmino Acid Sequence, Animals, Entropy, Humans, Kinetics, Ligands, Models, Chemical, Models, Molecular, Molecular Conformation, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Tertiary, Proteins
Abstract

<p>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.</p>

DOI10.1110/ps.072985007
Alternate JournalProtein Sci.
PubMed ID17962398
PubMed Central IDPMC2211703