Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.
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:
- Publisher copy:
- Copyright date:
If you are the owner of this record, you can report an update to it here: Report update to this record