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

Jannette Carey, Stina Lindman, Mikael Bauer, Sara Linse

Research output: Contribution to journalReview articlepeer-review

45 Scopus citations

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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)2317-2333
Number of pages17
JournalProtein Science
Volume16
Issue number11
DOIs
StatePublished - Nov 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Keywords

  • Cooperativity
  • Ligand binding
  • Metastability
  • Stability
  • Steric constraints

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