Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Salt-Induced Detour through Compact Regions of the Protein Folding Landscape

Otzen, Daniel E and Oliveberg, Mikael LU (1999) In Proceedings of the National Academy of Sciences 96(21). p.11746-11751
Abstract
In several cases, inorganic salts have been used to induce partly structured states in protein folding. But what is the nature of these states: Do they represent key stepping stones in the folding process, or are they circumstantial pitfalls in the energy landscape? Here we report that, in the case of the two-state protein S6, the salt-induced collapsed state is off the usual folding routes in the sense that it is prematurely collapsed and slows down folding by several orders of magnitude. Although this species is over-compact, it is not a dead-end trap but may fold by alternative channels to the native state.
Please use this url to cite or link to this publication:
author
and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Biochemistry
in
Proceedings of the National Academy of Sciences
volume
96
issue
21
pages
11746 - 11751
publisher
National Academy of Sciences
external identifiers
  • scopus:0032718386
ISSN
1091-6490
DOI
10.1073/pnas.96.21.11746
language
English
LU publication?
yes
id
7abe806c-d0d7-4a06-ac39-f483d5985a79 (old id 125365)
date added to LUP
2016-04-01 12:20:43
date last changed
2022-01-27 02:18:55
@article{7abe806c-d0d7-4a06-ac39-f483d5985a79,
  abstract     = {{In several cases, inorganic salts have been used to induce partly structured states in protein folding. But what is the nature of these states: Do they represent key stepping stones in the folding process, or are they circumstantial pitfalls in the energy landscape? Here we report that, in the case of the two-state protein S6, the salt-induced collapsed state is off the usual folding routes in the sense that it is prematurely collapsed and slows down folding by several orders of magnitude. Although this species is over-compact, it is not a dead-end trap but may fold by alternative channels to the native state.}},
  author       = {{Otzen, Daniel E and Oliveberg, Mikael}},
  issn         = {{1091-6490}},
  keywords     = {{Biochemistry}},
  language     = {{eng}},
  number       = {{21}},
  pages        = {{11746--11751}},
  publisher    = {{National Academy of Sciences}},
  series       = {{Proceedings of the National Academy of Sciences}},
  title        = {{Salt-Induced Detour through Compact Regions of the Protein Folding Landscape}},
  url          = {{http://dx.doi.org/10.1073/pnas.96.21.11746}},
  doi          = {{10.1073/pnas.96.21.11746}},
  volume       = {{96}},
  year         = {{1999}},
}