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Daniel Otzen

A simple way to measure protein refolding rates in water

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A simple way to measure protein refolding rates in water. / Otzen, Daniel E.; Oliveberg, Mikael.

In: Journal of Molecular Biology, Vol. 313, No. 3, 26.10.2001, p. 479-483.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Otzen, DE & Oliveberg, M 2001, 'A simple way to measure protein refolding rates in water', Journal of Molecular Biology, vol. 313, no. 3, pp. 479-483. https://doi.org/10.1006/jmbi.2001.5039

APA

Otzen, D. E., & Oliveberg, M. (2001). A simple way to measure protein refolding rates in water. Journal of Molecular Biology, 313(3), 479-483. https://doi.org/10.1006/jmbi.2001.5039

CBE

Otzen DE, Oliveberg M. 2001. A simple way to measure protein refolding rates in water. Journal of Molecular Biology. 313(3):479-483. https://doi.org/10.1006/jmbi.2001.5039

MLA

Otzen, Daniel E. and Mikael Oliveberg. "A simple way to measure protein refolding rates in water". Journal of Molecular Biology. 2001, 313(3). 479-483. https://doi.org/10.1006/jmbi.2001.5039

Vancouver

Otzen DE, Oliveberg M. A simple way to measure protein refolding rates in water. Journal of Molecular Biology. 2001 Oct 26;313(3):479-483. doi: 10.1006/jmbi.2001.5039

Author

Otzen, Daniel E. ; Oliveberg, Mikael. / A simple way to measure protein refolding rates in water. In: Journal of Molecular Biology. 2001 ; Vol. 313, No. 3. pp. 479-483.

Bibtex

@article{3f22222fd2864dad83a65560f57560d7,
title = "A simple way to measure protein refolding rates in water",
abstract = "Refolding of proteins is traditionally carried out either by diluting the denaturant-unfolded protein into buffer (GdmCl-jump) or by mixing the acid-denatured protein with strong buffer (pH-jump). The first method does not allow direct measurement of folding rates in water since the GdmCl cannot be infinitely diluted, and the second method suffers from the limitation that many proteins cannot be pH-denatured. Further, some proteins do not refold reversibly from low pH where they get trapped as aggregation prone intermediates. Here, we present an alternative approach for direct measurement of refolding rates in water, which does not rely on extrapolation. The protein is denatured in SDS, and is then mixed with α-cyclodextrin, which rapidly strips SDS molecules from the protein, leaving the naked unfolded protein to refold.",
keywords = "Chevron plots, Cyclodextrin, Protein folding, SDS, Stopped-flow",
author = "Otzen, {Daniel E.} and Mikael Oliveberg",
year = "2001",
month = oct,
day = "26",
doi = "10.1006/jmbi.2001.5039",
language = "English",
volume = "313",
pages = "479--483",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "3",

}

RIS

TY - JOUR

T1 - A simple way to measure protein refolding rates in water

AU - Otzen, Daniel E.

AU - Oliveberg, Mikael

PY - 2001/10/26

Y1 - 2001/10/26

N2 - Refolding of proteins is traditionally carried out either by diluting the denaturant-unfolded protein into buffer (GdmCl-jump) or by mixing the acid-denatured protein with strong buffer (pH-jump). The first method does not allow direct measurement of folding rates in water since the GdmCl cannot be infinitely diluted, and the second method suffers from the limitation that many proteins cannot be pH-denatured. Further, some proteins do not refold reversibly from low pH where they get trapped as aggregation prone intermediates. Here, we present an alternative approach for direct measurement of refolding rates in water, which does not rely on extrapolation. The protein is denatured in SDS, and is then mixed with α-cyclodextrin, which rapidly strips SDS molecules from the protein, leaving the naked unfolded protein to refold.

AB - Refolding of proteins is traditionally carried out either by diluting the denaturant-unfolded protein into buffer (GdmCl-jump) or by mixing the acid-denatured protein with strong buffer (pH-jump). The first method does not allow direct measurement of folding rates in water since the GdmCl cannot be infinitely diluted, and the second method suffers from the limitation that many proteins cannot be pH-denatured. Further, some proteins do not refold reversibly from low pH where they get trapped as aggregation prone intermediates. Here, we present an alternative approach for direct measurement of refolding rates in water, which does not rely on extrapolation. The protein is denatured in SDS, and is then mixed with α-cyclodextrin, which rapidly strips SDS molecules from the protein, leaving the naked unfolded protein to refold.

KW - Chevron plots

KW - Cyclodextrin

KW - Protein folding

KW - SDS

KW - Stopped-flow

UR - http://www.scopus.com/inward/record.url?scp=0035955556&partnerID=8YFLogxK

U2 - 10.1006/jmbi.2001.5039

DO - 10.1006/jmbi.2001.5039

M3 - Journal article

C2 - 11676533

AN - SCOPUS:0035955556

VL - 313

SP - 479

EP - 483

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -