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J Mol Biol. 1995 Nov 10;253(5):651-7.

Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.

Author information

1
Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge 02142, USA.

Abstract

alpha-Lactalbumin (alpha-LA) is a two-domain, calcium-binding protein that forms one of the best studied molten globules. We present here amide hydrogen exchange studies of the molten globule formed by human alpha-LA at pH 2 and compare these results with a similar study of the native state at pH 6.3. The most persistent structure in the molten globule is localized in the helical domain, consistent with previous results. However, the helices most protected from hydrogen exchange in the molten globule are, in the native state, less protected from exchange than other regions of the protein. The molten globule appears to contain major elements of the native fold, but formation of the fully native state requires stabilization of structure around the calcium-binding site and domain interface.

PMID:
7473740
DOI:
10.1006/jmbi.1995.0579
[Indexed for MEDLINE]

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