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Structural basis of...
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Morozova, Ludmilla A,1956-Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford
(author)
Structural basis of the stability of a lysozyme molten globule.
- Article/chapterEnglish1995
Publisher, publication year, extent ...
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Nature Publishing Group,1995
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:umu-43011
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-43011URI
Supplementary language notes
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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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.
Added entries (persons, corporate bodies, meetings, titles ...)
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Haynie, Donald T
(author)
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Arico-Muendel, Christopher
(author)
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Van Dael, Herman
(author)
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Dobson, Christopher M
(author)
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Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford
(creator_code:org_t)
Related titles
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In:Nature Structural Biology: Nature Publishing Group2:10, s. 871-8751072-8368
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