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Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH

Nature Structural Biology volume 3, pages 782–787 (1996)Cite this article

An Erratum to this article was published on 01 December 1996

Abstract

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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Authors and Affiliations

  1. Department of Molecular and Cell Biology, University of California, Berkeley, 229 Stanley Hall, Berkeley, California, 94720, USA

    Aaron K. Chamberlain, Tracy M. Handel & Susan Marqusee

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  1. Aaron K. Chamberlain
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  2. Tracy M. Handel
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  3. Susan Marqusee
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Chamberlain, A., Handel, T. & Marqusee, S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nat Struct Mol Biol 3, 782–787 (1996). https://doi.org/10.1038/nsb0996-782

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