Salt-Induced Detour through Compact Regions of the Protein Folding Landscape
(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:
https://lup.lub.lu.se/record/125365
- author
- Otzen, Daniel E and Oliveberg, Mikael LU
- organization
- publishing date
- 1999
- 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}}, }