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

Carey, Jannette ; Lindman, Stina LU ; Bauer, Mikael LU and Linse, Sara LU (2007) In Protein Science 16(11). p.2317-2333
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.
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
metastability, stability, steric constraints, ligand, cooperativity, binding
in
Protein Science
volume
16
issue
11
pages
2317 - 2333
publisher
The Protein Society
external identifiers
  • wos:000250444400001
  • scopus:35648930538
ISSN
1469-896X
DOI
10.1110/ps.072985007
language
English
LU publication?
yes
id
c5221548-daf5-4514-b752-e4e00fcc57be (old id 651797)
date added to LUP
2016-04-01 11:56:31
date last changed
2022-02-18 07:35:53
@article{c5221548-daf5-4514-b752-e4e00fcc57be,
  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.}},
  author       = {{Carey, Jannette and Lindman, Stina and Bauer, Mikael and Linse, Sara}},
  issn         = {{1469-896X}},
  keywords     = {{metastability; stability; steric constraints; ligand; cooperativity; binding}},
  language     = {{eng}},
  number       = {{11}},
  pages        = {{2317--2333}},
  publisher    = {{The Protein Society}},
  series       = {{Protein Science}},
  title        = {{Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency}},
  url          = {{http://dx.doi.org/10.1110/ps.072985007}},
  doi          = {{10.1110/ps.072985007}},
  volume       = {{16}},
  year         = {{2007}},
}