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The burst phase in ribonuclease A folding and solvent dependence of the unfolded state
P X Qi1, T R Sosnick, S W Englander
1The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104-6059, USA. Phoebe@HX2.Med.UPenn.Edu
Nature Structural Biology
|October 23, 1998
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.