CONFORMATION OF GROEL-BOUND ALPHA-LACTALBUMIN PROBED BY MASS-SPECTROMETRY

Citation
Cv. Robinson et al., CONFORMATION OF GROEL-BOUND ALPHA-LACTALBUMIN PROBED BY MASS-SPECTROMETRY, Nature, 372(6507), 1994, pp. 646-651
Citations number
51
Categorie Soggetti
Multidisciplinary Sciences
Journal title
NatureACNP
ISSN journal
00280836
Volume
372
Issue
6507
Year of publication
1994
Pages
646 - 651
Database
ISI
SICI code
0028-0836(1994)372:6507<646:COGAPB>2.0.ZU;2-Y
Abstract
The conformation of a three-disulphide derivative of bovine alpha-lact albumin bound to the molecular chaperone GroEL has been investigated b y monitoring directly its hydrogen exchange kinetics using electrospra y ionization mass spectrometry. The bound protein is weakly protected from exchange to an extent closely similar to that of an uncomplexed m olten globule state of the three-disulphide protein. Binding to GroEL in this system appears to involve relatively disordered partly folded states resembling intermediates formed in the very early stages of kin etic folding of many proteins in vitro.