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

Published online by Cambridge University Press:  08 December 2000

LELAND MAYNE  and
S. WALTER ENGLANDER
LELAND MAYNE
Affiliation:
The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104
S. WALTER ENGLANDER
Affiliation:
The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104
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Abstract

A 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.

Keywords

cytochrome cfoldinghydrogen exchangestabilitymeltingtwo-state
Type
Research Article
Information
Protein Science , Volume 9 , Issue 10 , October 2000 , pp. 1873 - 1877
Copyright
© 2000 The Protein Society

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