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Structural basis of the stability of a lysozyme molten globule

Nature Structural Biology volume 2, pages 871–875 (1995)Cite this article

Abstract

Hydrogen exchange measurements on equine lysozyme show that amides in three of the four major helices of the native protein are significantly protected in a molten globule state formed at pH 2. The pattern of protection within the different helices, however, varies significantly. Examination of the pattern in the light of the native structure indicates that the side chains of the protected residues form a compact cluster within the core of the protein. We suggest that such a core is present in the molten globule state, indicating the existence of substantial native-like interactions between hydrophobic residues. The formation of clusters of this type during the early stages of folding could be crucial to directing polypeptide chains to their native structures.

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Author notes

  1. Christopher Arico-Muendel

    Present address: Department of Chemistry, Brandeis University, Waltham, Massachusetts, 02254, USA

Authors and Affiliations

  1. Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, UK

    Ludmilla A. Morozova, Donald T. Haynie, Christopher Arico-Muendel & Christopher M. Dobson

  2. On leave of absence from the Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142292, Pushchino, Moscow Region, Russia

    Ludmilla A. Morozova

  3. Interdisciplinary Research Centre, K.U. Leuven Campus Kortrijk, B-8500, Kortrijk, Belgium

    Herman Van Dael

Authors
  1. Ludmilla A. Morozova
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  2. Donald T. Haynie
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  3. Christopher Arico-Muendel
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  4. Herman Van Dael
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  5. Christopher M. Dobson
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Morozova, L., Haynie, D., Arico-Muendel, C. et al. Structural basis of the stability of a lysozyme molten globule. Nat Struct Mol Biol 2, 871–875 (1995). https://doi.org/10.1038/nsb1095-871

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