DOI: 10.1110/ps.9.10.1873. Two‐state vs. multistate protein unfolding studied by optical melting and hydrogen exchange

Two‐state vs. multistate protein unfolding studied by optical melting and hydrogen exchange

10.1110/ps.9.10.1873

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractA direct conflict between the stabilization free energy parameters of cytochrome c determined by optical methods and by hydrogen exchange (HX) is quantitatively explained when the partially folded intermediates seen by HX are taken into account. The results support the previous HX measurements of intermediate populations, show how intermediates can elude the standard melting analysis, and illustrate how they confuse the analysis when they are significantly populated within the melting transition region.

Bibliography

Mayne, L., & Englander, S. W. (2000). Twoâstate vs. multistate protein unfolding studied by optical melting and hydrogen exchange. Protein Science, 9(10), 1873â1877. Portico.

Authors 2

Leland Mayne (first)
S. Walter Englander (additional)

References 26 Referenced 57

10.1021/bi00839a053
10.1002/prot.340200103
10.1016/0076-6879(95)59051-X
10.1126/science.7618079
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10.1038/1810

Dates

Type	When
Created	16 years, 6 months ago (Feb. 17, 2009, 5:48 p.m.)
Deposited	1 year, 10 months ago (Oct. 29, 2023, 1:36 p.m.)
Indexed	4 months ago (May 6, 2025, 1:09 p.m.)
Issued	25 years, 8 months ago (Jan. 1, 2000)
Published	25 years, 8 months ago (Jan. 1, 2000)
Published Online	16 years, 8 months ago (Dec. 31, 2008)
Published Print	25 years, 8 months ago (Jan. 1, 2000)

Funders 0

None

BibTeX

@article{Mayne_2000, title={Two‐state vs. multistate protein unfolding studied by optical melting and hydrogen exchange}, volume={9}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.9.10.1873}, DOI={10.1110/ps.9.10.1873}, number={10}, journal={Protein Science}, publisher={Wiley}, author={Mayne, Leland and Englander, S. Walter}, year={2000}, month=jan, pages={1873–1877} }

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