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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Schulman BA,Redfield C,Peng ZY,Dobson CM,Kim PSdoi
10.1006/jmbi.1995.0579subject
Has Abstractpub_date
1995-11-10 00:00:00pages
651-7issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(85)70579-7journal_volume
253pub_type
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