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Daniel Otzen

Burst-phase expansion of native protein prior to global unfolding in SDS

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Burst-phase expansion of native protein prior to global unfolding in SDS. / Otzen, Daniel E.; Oliveberg, Mikael.

In: Journal of Molecular Biology, Vol. 315, No. 5, 01.01.2002, p. 1231-1240.

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

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Otzen, DE & Oliveberg, M 2002, 'Burst-phase expansion of native protein prior to global unfolding in SDS', Journal of Molecular Biology, vol. 315, no. 5, pp. 1231-1240. https://doi.org/10.1006/jmbi.2001.5300

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Otzen, Daniel E. ; Oliveberg, Mikael. / Burst-phase expansion of native protein prior to global unfolding in SDS. In: Journal of Molecular Biology. 2002 ; Vol. 315, No. 5. pp. 1231-1240.

Bibtex

@article{5c49aa688c6e4d1886368a7d8c9658ea,
title = "Burst-phase expansion of native protein prior to global unfolding in SDS",
abstract = "Although numerous studies have been directed at understanding early folding events through the characterization of folding intermediates, there are few reports on the very late folding events, i.e. on the events taking place on the native side of the folding barrier and on alternative conformations of the folded state. To shed further light on these issues, we have characterized by protein engineering the structure of an expanded but native-like intermediate that accumulates transiently in the unfolding reaction of the small protein S6 in the presence of SDS. The results show that the SDS micelles attack the native protein in the dead-time of the denaturation experiment, causing an expansion of the hydrophobic core prior to the major unfolding transition. We distinguish two forms of the unfolding intermediate that are correlated with the micellar structure. With spherical micelles, the expansion is seen mainly as a weakening of the interactions which anchor the two α-helices to the core of the S6 structure. With cylindrical micelles, prevalent at higher SDS concentrations, the expansion is more global and produces a species which closely resembles the transition-state structure for unfolding in GdmCl. Despite the highly weakened core, the micelle-associated intermediate displays cooperative unfolding, indicating a significant structural plasticity of the species on the native side of the folding barrier in the presence of SDS.",
keywords = "Detergent, Phi-value analysis, Protein folding, Sodium dodecyl sulfate, Unfolding intermediate",
author = "Otzen, {Daniel E.} and Mikael Oliveberg",
year = "2002",
month = jan,
day = "1",
doi = "10.1006/jmbi.2001.5300",
language = "English",
volume = "315",
pages = "1231--1240",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "5",

}

RIS

TY - JOUR

T1 - Burst-phase expansion of native protein prior to global unfolding in SDS

AU - Otzen, Daniel E.

AU - Oliveberg, Mikael

PY - 2002/1/1

Y1 - 2002/1/1

N2 - Although numerous studies have been directed at understanding early folding events through the characterization of folding intermediates, there are few reports on the very late folding events, i.e. on the events taking place on the native side of the folding barrier and on alternative conformations of the folded state. To shed further light on these issues, we have characterized by protein engineering the structure of an expanded but native-like intermediate that accumulates transiently in the unfolding reaction of the small protein S6 in the presence of SDS. The results show that the SDS micelles attack the native protein in the dead-time of the denaturation experiment, causing an expansion of the hydrophobic core prior to the major unfolding transition. We distinguish two forms of the unfolding intermediate that are correlated with the micellar structure. With spherical micelles, the expansion is seen mainly as a weakening of the interactions which anchor the two α-helices to the core of the S6 structure. With cylindrical micelles, prevalent at higher SDS concentrations, the expansion is more global and produces a species which closely resembles the transition-state structure for unfolding in GdmCl. Despite the highly weakened core, the micelle-associated intermediate displays cooperative unfolding, indicating a significant structural plasticity of the species on the native side of the folding barrier in the presence of SDS.

AB - Although numerous studies have been directed at understanding early folding events through the characterization of folding intermediates, there are few reports on the very late folding events, i.e. on the events taking place on the native side of the folding barrier and on alternative conformations of the folded state. To shed further light on these issues, we have characterized by protein engineering the structure of an expanded but native-like intermediate that accumulates transiently in the unfolding reaction of the small protein S6 in the presence of SDS. The results show that the SDS micelles attack the native protein in the dead-time of the denaturation experiment, causing an expansion of the hydrophobic core prior to the major unfolding transition. We distinguish two forms of the unfolding intermediate that are correlated with the micellar structure. With spherical micelles, the expansion is seen mainly as a weakening of the interactions which anchor the two α-helices to the core of the S6 structure. With cylindrical micelles, prevalent at higher SDS concentrations, the expansion is more global and produces a species which closely resembles the transition-state structure for unfolding in GdmCl. Despite the highly weakened core, the micelle-associated intermediate displays cooperative unfolding, indicating a significant structural plasticity of the species on the native side of the folding barrier in the presence of SDS.

KW - Detergent

KW - Phi-value analysis

KW - Protein folding

KW - Sodium dodecyl sulfate

KW - Unfolding intermediate

UR - http://www.scopus.com/inward/record.url?scp=0036307492&partnerID=8YFLogxK

U2 - 10.1006/jmbi.2001.5300

DO - 10.1006/jmbi.2001.5300

M3 - Journal article

C2 - 11827490

AN - SCOPUS:0036307492

VL - 315

SP - 1231

EP - 1240

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 5

ER -