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The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

Kragelund, B B; Osmark, Peter LU ; Neergaard, T B; Schiodt, J; Kristiansen, K; Knudsen, J and Poulsen, F M (1999) In Nature Structural Biology 6(6). p.594-601
Abstract
The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Nature Structural Biology
volume
6
issue
6
pages
594 - 601
publisher
Nature Publishing Group
external identifiers
  • pmid:10360367
  • scopus:0033015989
ISSN
1072-8368
DOI
10.1038/9384
language
English
LU publication?
no
id
1fff2182-fa32-4be4-a44d-05b43cebcd5a (old id 1114284)
date added to LUP
2008-07-03 16:12:31
date last changed
2017-09-17 08:03:00
@article{1fff2182-fa32-4be4-a44d-05b43cebcd5a,
  abstract     = {The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.},
  author       = {Kragelund, B B and Osmark, Peter and Neergaard, T B and Schiodt, J and Kristiansen, K and Knudsen, J and Poulsen, F M},
  issn         = {1072-8368},
  language     = {eng},
  number       = {6},
  pages        = {594--601},
  publisher    = {Nature Publishing Group},
  series       = {Nature Structural Biology},
  title        = {The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP},
  url          = {http://dx.doi.org/10.1038/9384},
  volume       = {6},
  year         = {1999},
}