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Daniel Otzen

Conformational detours during folding of a collapsed state

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Conformational detours during folding of a collapsed state. / Otzen, Daniel E.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1750, No. 2, 30.06.2005, p. 146-153.

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

Harvard

Otzen, DE 2005, 'Conformational detours during folding of a collapsed state', Biochimica et Biophysica Acta - Proteins and Proteomics, vol. 1750, no. 2, pp. 146-153. https://doi.org/10.1016/j.bbapap.2005.05.006

APA

Otzen, D. E. (2005). Conformational detours during folding of a collapsed state. Biochimica et Biophysica Acta - Proteins and Proteomics, 1750(2), 146-153. https://doi.org/10.1016/j.bbapap.2005.05.006

CBE

Otzen DE. 2005. Conformational detours during folding of a collapsed state. Biochimica et Biophysica Acta - Proteins and Proteomics. 1750(2):146-153. https://doi.org/10.1016/j.bbapap.2005.05.006

MLA

Otzen, Daniel E. "Conformational detours during folding of a collapsed state". Biochimica et Biophysica Acta - Proteins and Proteomics. 2005, 1750(2). 146-153. https://doi.org/10.1016/j.bbapap.2005.05.006

Vancouver

Otzen DE. Conformational detours during folding of a collapsed state. Biochimica et Biophysica Acta - Proteins and Proteomics. 2005 Jun 30;1750(2):146-153. https://doi.org/10.1016/j.bbapap.2005.05.006

Author

Otzen, Daniel E. / Conformational detours during folding of a collapsed state. In: Biochimica et Biophysica Acta - Proteins and Proteomics. 2005 ; Vol. 1750, No. 2. pp. 146-153.

Bibtex

@article{a23e747fda2c4fde9b9afeef5b5682ce,
title = "Conformational detours during folding of a collapsed state",
abstract = "The protein S6 is a useful model to probe the role of partially folded states in the folding process. In the absence of salt, S6 folds from the denatured state D to the native state N without detectable intermediates. High concentrations of sodium sulfate induce the accumulation of a collapsed state C, which is off the direct folding route. However, the mutation VA85 enables S6 to fold from C directly to N through the transition state TSC. According to the denaturant dependence of this reaction, TSC and C are equally compact, but the data are difficult to deconvolute. Therefore, I have measured the heat capacities (ΔCp) for the D→C and C→TSC transitions. The ΔCp-values suggest that C needs to increase its surface area in order to fold directly to N. This underlines that it is a misfolded state that can only fold by at least partial unfolding. In contrast to the C-state formed by S6 wildtype, the VA85 C-state is just as compact as the native state, and this may be a prerequisite for direct folding. Individual {"}gatekeeper{"} residues may thus play a disproportionately large role in guiding proteins through different folding pathways.",
keywords = "Detour, Energy landscape, Heat capacity, Intermediate, Misfolded state, Protein folding",
author = "Otzen, {Daniel E.}",
year = "2005",
month = jun,
day = "30",
doi = "10.1016/j.bbapap.2005.05.006",
language = "English",
volume = "1750",
pages = "146--153",
journal = "B B A - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier BV",
number = "2",

}

RIS

TY - JOUR

T1 - Conformational detours during folding of a collapsed state

AU - Otzen, Daniel E.

PY - 2005/6/30

Y1 - 2005/6/30

N2 - The protein S6 is a useful model to probe the role of partially folded states in the folding process. In the absence of salt, S6 folds from the denatured state D to the native state N without detectable intermediates. High concentrations of sodium sulfate induce the accumulation of a collapsed state C, which is off the direct folding route. However, the mutation VA85 enables S6 to fold from C directly to N through the transition state TSC. According to the denaturant dependence of this reaction, TSC and C are equally compact, but the data are difficult to deconvolute. Therefore, I have measured the heat capacities (ΔCp) for the D→C and C→TSC transitions. The ΔCp-values suggest that C needs to increase its surface area in order to fold directly to N. This underlines that it is a misfolded state that can only fold by at least partial unfolding. In contrast to the C-state formed by S6 wildtype, the VA85 C-state is just as compact as the native state, and this may be a prerequisite for direct folding. Individual "gatekeeper" residues may thus play a disproportionately large role in guiding proteins through different folding pathways.

AB - The protein S6 is a useful model to probe the role of partially folded states in the folding process. In the absence of salt, S6 folds from the denatured state D to the native state N without detectable intermediates. High concentrations of sodium sulfate induce the accumulation of a collapsed state C, which is off the direct folding route. However, the mutation VA85 enables S6 to fold from C directly to N through the transition state TSC. According to the denaturant dependence of this reaction, TSC and C are equally compact, but the data are difficult to deconvolute. Therefore, I have measured the heat capacities (ΔCp) for the D→C and C→TSC transitions. The ΔCp-values suggest that C needs to increase its surface area in order to fold directly to N. This underlines that it is a misfolded state that can only fold by at least partial unfolding. In contrast to the C-state formed by S6 wildtype, the VA85 C-state is just as compact as the native state, and this may be a prerequisite for direct folding. Individual "gatekeeper" residues may thus play a disproportionately large role in guiding proteins through different folding pathways.

KW - Detour

KW - Energy landscape

KW - Heat capacity

KW - Intermediate

KW - Misfolded state

KW - Protein folding

UR - http://www.scopus.com/inward/record.url?scp=20644450354&partnerID=8YFLogxK

U2 - 10.1016/j.bbapap.2005.05.006

DO - 10.1016/j.bbapap.2005.05.006

M3 - Journal article

C2 - 15955750

AN - SCOPUS:20644450354

VL - 1750

SP - 146

EP - 153

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

SN - 1570-9639

IS - 2

ER -