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Structural basis of the stability of a lysozyme molten globule.
Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford.
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1995 (English)In: Nature Structural Biology, ISSN 1072-8368, Vol. 2, no 10, 871-875 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Nature Publishing Group , 1995. Vol. 2, no 10, 871-875 p.
URN: urn:nbn:se:umu:diva-43011PubMedID: 7552711OAI: diva2:411104
Available from: 2011-04-18 Created: 2011-04-15 Last updated: 2011-04-18Bibliographically approved

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Morozova, Ludmilla A
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