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GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

Abstract:

The chaperonin GroEL binds folding intermediates of four-disulfidehen lysozyme transiently within its central cavity. Using stopped flow fluorescence we show that GroEL binds early intermediates in folding and accelerates the slow kinetic phase that reflects the reversal of non-native interactions involving tryptophan residues and the formation of the native state. Pulsed hydrogen exchange monitored by electrospray ionization mass spectrometry demonstrates that GroEL does not alter the foldin...

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Publication status:
Published

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Publisher copy:
10.1038/10735

Authors


Texter, FL More by this author
Ashcroft, AE More by this author
Masselos, D More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
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Journal:
Nature structural biology
Volume:
6
Issue:
7
Pages:
683-690
Publication date:
1999-07-05
DOI:
ISSN:
1072-8368
URN:
uuid:7a796c7b-91b8-488d-b3ab-f0d89ddc5df4
Source identifiers:
59384
Local pid:
pubs:59384

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