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Mapping the structure of a non-native state of staphylococcal nuclease

Nature Structural Biology volume 3, pages 59–66 (1996)Cite this article

Abstract

Non-native states of proteins populated at extremes of pH, or by mutation or truncation of the protein sequence, are thought to be equilibrium models for kinetic intermediates on the folding pathway. While the global physical properties of these molecules have been well characterized, analysis of their structure by NMR spectroscopy has proven difficult. Here we report the use of a new chemical cleavage technique, based on reactive oxygen species, to map the backbone fold of a truncated form of staphylococcal nuclease in a non-native state. The fragment adopts a native-like fold, however the technique also reveals regions of non-native structure.

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Author information

Author notes

  1. David W. Ledman & Robert O. Fox

    Present address: The Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch at Galveston, Galveston, Texas, 77555, USA

Authors and Affiliations

  1. The Howard Hughes Medical Institute, Yale University, 266 Whitney Avenue, New Haven, Connecticut, 06520, USA

    Mario R. Ermácora & Robert O. Fox

  2. The Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, Connecticut, 06520, USA

    Mario R. Ermácora, David W. Ledman & Robert O. Fox

  3. Instituto de Química y Fisicoquímica Biológicas, Facultad de Farmacia y Bioqumica (UBA-CONICET), Buenos Aires, Argentina

    Mario R. Ermácora

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Ermácora, M., Ledman, D. & Fox, R. Mapping the structure of a non-native state of staphylococcal nuclease. Nat Struct Mol Biol 3, 59–66 (1996). https://doi.org/10.1038/nsb0196-59

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