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Characterization of an alternative low energy fold for bovine α-lactalbumin formed by disulfide bond shuffling.

Abstract:

Bovine α-lactalbumin (αLA) forms a misfolded disulfide bond shuffled isomer, X-αLA. This X-αLA isomer contains two native disulfide bridges (Cys 6-Cys 120 and Cys 28-Cys 111) and two non-native disulfide bridges (Cys 61-Cys 73 and Cys 77-Cys 91). MD simulations have been used to characterize the X-αLA isomer and its formation via disulfide bond shuffling and to compare it with the native fold of αLA. In the simulations of the X-αLA isomer the structure of the α-domain of native αLA is largely...

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Publication status:
Published

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Publisher copy:
10.1002/prot.23247

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Proteins
Volume:
80
Issue:
3
Pages:
913-919
Publication date:
2012-03-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:3411f657-9ceb-4552-836e-100afe60a086
Source identifiers:
221312
Local pid:
pubs:221312

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