Hostname: page-component-78c5997874-g7gxr Total loading time: 0 Render date: 2024-11-08T15:31:00.269Z Has data issue: false hasContentIssue false

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

Published online by Cambridge University Press:  08 December 2000

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
Get access

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.

Type
Research Article
Copyright
© 2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)