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Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry.

Abstract:

The hydrogen-exchange behavior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has been examined and compared with that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants of [28-111] alpha-lactalbumin. The small differences in hydrogen-exchange protection exhibited by these partially folded species were compared by mixing two or more proteins and monitoring their exchange simultaneously using mass spectrometr...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.2001.4911

Authors


Schulman, BA More by this author
Robinson, CV More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Journal of molecular biology
Volume:
311
Issue:
4
Pages:
909-919
Publication date:
2001-08-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:306674e9-6acf-4abf-866e-7f8198e4b3aa
Source identifiers:
59233
Local pid:
pubs:59233

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