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Conformational properties of the unfolded state of Im7 in nondenaturing conditions.

Abstract:

The unfolded ensemble in aqueous solution represents the starting point of protein folding. Characterisation of this species is often difficult since the native state is usually predominantly populated at equilibrium. Previous work has shown that the four-helix protein, Im7 (immunity protein 7), folds via an on-pathway intermediate. While the transition states and folding intermediate have been characterised in atomistic detail, knowledge of the unfolded ensemble under the same ambient condit...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2011.12.041

Authors


Pashley, CL More by this author
Morgan, GJ More by this author
Kalverda, AP More by this author
Thompson, GS More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
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Journal:
Journal of molecular biology
Volume:
416
Issue:
2
Pages:
300-318
Publication date:
2012-02-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:4f9be73d-aa41-4686-83ab-9a6c4b196816
Source identifiers:
310238
Local pid:
pubs:310238

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