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Nat Struct Biol. 1998 Oct;5(10):882-4.

The burst phase in ribonuclease A folding and solvent dependence of the unfolded state.

Author information

1
The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104-6059, USA. Phoebe@HX2.Med.UPenn.Edu

Abstract

Submillisecond burst phase signals measured in kinetic protein folding experiments have been widely interpreted in terms of the fast formation of productive folding intermediates. Experimental comparisons with non-folding polypeptide chains show that, for ribonuclease A and cytochrome c, these signals in fact reflect a shift from one biased ensemble of the unfolded state to another as a function of change in denaturant concentration.

PMID:
9783747
DOI:
10.1038/2321
[Indexed for MEDLINE]

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