Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.
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.
Carey
Jannette
J
Chemistry Department, Princeton University, NJ 08544-1009, USA. jcarey@princeton.edu
Lindman
Stina
S
Bauer
Mikael
M
Linse
Sara
S
D000595:Amino Acid Sequence; D000818:Animals; D019277:Entropy; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
D008024:Ligands; D011506:Proteins