- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/prot.23247
-
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2012
Journal article
Characterization of an alternative low energy fold for bovine α-lactalbumin formed by disulfide bond shuffling.
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