Structural basis of the stability of a lysozyme molten globule.

Morozova, Ludmilla A, 1956- (author): Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford

Haynie, Donald T (author)

Arico-Muendel, Christopher (author)

Van Dael, Herman (author)

Dobson, Christopher M (author)

(creator_code:org_t)

Nature Publishing Group, 1995
1995
English.
In: Nature Structural Biology. - : Nature Publishing Group. - 1072-8368. ; 2:10, s. 871-875

Abstract Subject headings

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.

By the author/editor: Morozova, Ludmil ...; Haynie, Donald T; Arico-Muendel, C ...; Van Dael, Herman; Dobson, Christop ...

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