- Abstract:
-
The unfolding of the apo and holo forms of bovine alpha-lactalbumin (alpha-LA) upon reduction by dithiothreitol (DTT) in the presence of the small heat-shock protein alpha-crystallin, a molecular chaperone, has been monitored by visible and UV absorption spectroscopy, mass spectrometry and (1)H NMR spectroscopy. From these data, a description and a time-course of the events that result from the unfolding of both forms of the protein, and the state of the protein that interacts with alpha-crys...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/s0022-2836(02)00144-4
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- Journal:
- Journal of molecular biology
- Volume:
- 318
- Issue:
- 3
- Pages:
- 815-827
- Publication date:
- 2002-05-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:b53fb0e9-bb90-4a9a-9029-0f612b87274b
- Source identifiers:
-
100594
- Local pid:
- pubs:100594
- Language:
- English
- Keywords:
- Copyright date:
- 2002
Journal article
The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study.
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