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Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling.

Abstract:

An unresolved key issue in the mechanism of protein folding assisted by the molecular chaperone GroEL is the nature of the substrate protein bound to the chaperonin at different stages of its reaction cycle. Here we describe the conformational properties of human dihydrofolate reductase (DHFR) bound to GroEL at different stages of its ATP-driven folding reaction, determined by hydrogen exchange labeling and electrospray ionization mass spectrometry. Considerable protection involving about 20 ...

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Publication status:
Published

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Publisher copy:
10.1002/pro.5560051213

Authors


Robinson, CV More by this author
Radford, SE More by this author
Journal:
Protein science : a publication of the Protein Society
Volume:
5
Issue:
12
Pages:
2506-2513
Publication date:
1996-12-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:a70600a5-57fc-4d94-8dfa-0a0e1404b063
Source identifiers:
59350
Local pid:
pubs:59350

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