Journal article icon

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 ...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1038/372646a0

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Ewbank, JJ More by this author
Expand authors...
Journal:
Nature
Volume:
372
Issue:
6507
Pages:
646-651
Publication date:
1994-12-05
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
URN:
uuid:703dcb6b-dffd-477d-b6dd-1401c403b69a
Source identifiers:
59345
Local pid:
pubs:59345

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP