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

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 Biol

authors

Schulman BA,Redfield C,Peng ZY,Dobson CM,Kim PS

doi

10.1006/jmbi.1995.0579

subject

Has Abstract

pub_date

1995-11-10 00:00:00

pages

651-7

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(85)70579-7

journal_volume

253

pub_type

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