Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry Journal Article
| Authors: | Robinson, C. V.; Groß, M.; Eyles, S. J.; Ewbank, J. J.; Mayhew, M.; Hartl, F. U.; Dobson, C. M.; Radford, S. E. |
| Article Title: | Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry |
| Abstract: | The conformation of a three-disulphide derivative of bovine α-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. © 2002 Nature Publishing Group. |
| Keywords: | nonhuman; protein conformation; mass spectrometry; animal; protein binding; kinetics; escherichia coli; cattle; protein folding; disulfides; chaperone; hydrogen; chemical reaction kinetics; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; spectrum analysis, mass; groel protein; lactalbumin; alpha lactalbumin |
| Journal Title: | Nature |
| Volume: | 372 |
| Issue: | 6507 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1994-12-15 |
| Start Page: | 646 |
| End Page: | 651 |
| Language: | English |
| DOI: | 10.1038/372646a0 |
| PROVIDER: | scopus |
| PUBMED: | 7990955 |
| DOI/URL: | |
| Notes: | Cited By :181 -- Export Date: 14 January 2019 -- Article -- Source: Scopus |
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