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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 resembling intermediates formed in the very early stages of kinetic folding of many proteins in vitro.

Original publication

DOI

10.1038/372646a0

Type

Journal article

Journal

Nature

Publication Date

15/12/1994

Volume

372

Pages

646 - 651

Keywords

Animals, Cattle, Chaperonin 60, Disulfides, Escherichia coli, Hydrogen, Kinetics, Lactalbumin, Mass Spectrometry, Protein Binding, Protein Conformation