Nature Structural Biology
3, 782 - 787 (1996)
doi:10.1038/nsb0996-782
Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseHAaron K. Chamberlain1, Tracy M. Handel1
& Susan Marqusee1
1Department of Molecular and Cell Biology, 229 Stanley Hall, University of California, Berkeley Berkeley, California 94720 USA Despite the general observation that single domain proteins denature in a completely cooperative manner, amide hydrogen exchange of ribonuclease H in low levels of denaturant demonstrates the existence of two partially folded species. The structures of these marginally stable species resemble kinetic folding intermediates and the molten globule state of the protein. These data suggest that the first region to fold is the thermodynamically most stable portion of the protein and that the molten globule is a high free energy conformation present at equilibrium in the native state.
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