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Daniel Otzen

Salt-induced detour through compact regions of the protein folding landscape

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Salt-induced detour through compact regions of the protein folding landscape. / Otzen, Daniel E.; Oliveberg, Mikael.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 21, 12.10.1999, p. 11746-11751.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Otzen, DE & Oliveberg, M 1999, 'Salt-induced detour through compact regions of the protein folding landscape', Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 21, pp. 11746-11751. https://doi.org/10.1073/pnas.96.21.11746

APA

Otzen, D. E., & Oliveberg, M. (1999). Salt-induced detour through compact regions of the protein folding landscape. Proceedings of the National Academy of Sciences of the United States of America, 96(21), 11746-11751. https://doi.org/10.1073/pnas.96.21.11746

CBE

Otzen DE, Oliveberg M. 1999. Salt-induced detour through compact regions of the protein folding landscape. Proceedings of the National Academy of Sciences of the United States of America. 96(21):11746-11751. https://doi.org/10.1073/pnas.96.21.11746

MLA

Otzen, Daniel E. and Mikael Oliveberg. "Salt-induced detour through compact regions of the protein folding landscape". Proceedings of the National Academy of Sciences of the United States of America. 1999, 96(21). 11746-11751. https://doi.org/10.1073/pnas.96.21.11746

Vancouver

Otzen DE, Oliveberg M. Salt-induced detour through compact regions of the protein folding landscape. Proceedings of the National Academy of Sciences of the United States of America. 1999 Oct 12;96(21):11746-11751. https://doi.org/10.1073/pnas.96.21.11746

Author

Otzen, Daniel E. ; Oliveberg, Mikael. / Salt-induced detour through compact regions of the protein folding landscape. In: Proceedings of the National Academy of Sciences of the United States of America. 1999 ; Vol. 96, No. 21. pp. 11746-11751.

Bibtex

@article{7b81de5ad1904c0e88481d7871ccb7cb,
title = "Salt-induced detour through compact regions of the protein folding landscape",
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.",
keywords = "2-state, Collapse, Intermediate, Protein engineering",
author = "Otzen, {Daniel E.} and Mikael Oliveberg",
year = "1999",
month = oct,
day = "12",
doi = "10.1073/pnas.96.21.11746",
language = "English",
volume = "96",
pages = "11746--11751",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "21",

}

RIS

TY - JOUR

T1 - Salt-induced detour through compact regions of the protein folding landscape

AU - Otzen, Daniel E.

AU - Oliveberg, Mikael

PY - 1999/10/12

Y1 - 1999/10/12

N2 - 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.

AB - 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.

KW - 2-state

KW - Collapse

KW - Intermediate

KW - Protein engineering

UR - http://www.scopus.com/inward/record.url?scp=0032718386&partnerID=8YFLogxK

U2 - 10.1073/pnas.96.21.11746

DO - 10.1073/pnas.96.21.11746

M3 - Journal article

C2 - 10518521

AN - SCOPUS:0032718386

VL - 96

SP - 11746

EP - 11751

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 21

ER -