- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1006/jmbi.2001.4911
-
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- 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
- Copyright date:
- 2001
Journal article
Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry.
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