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Journal article

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

Abstract:

The conformation of a three-disulphide derivative of bovine alpha-lactalbumin bound to the molecular chaperone GroEL has been investigated by monitoring directly its hydrogen exchange kinetics using electrospray ionization mass spectrometry. The bound protein is weakly protected from exchange to an extent closely similar to that of an uncomplexed molten globule state of the three-disulphide protein. Binding to GroEL in this system appears to involve relatively disordered partly folded states ...

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Publication status:
Published

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Publisher copy:
10.1038/372646a0

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
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Journal:
Nature
Volume:
372
Issue:
6507
Pages:
646-651
Publication date:
1994-12-01
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
Source identifiers:
59345
Language:
English
Keywords:
Pubs id:
pubs:59345
UUID:
uuid:703dcb6b-dffd-477d-b6dd-1401c403b69a
Local pid:
pubs:59345
Deposit date:
2012-12-19

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