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

Pub. Date : 2012 Mar

PMID : 22189830






8 Functional Relationships(s)
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1 Characterization of an alternative low energy fold for bovine alpha-lactalbumin formed by disulfide bond shuffling. Disulfides lactalbumin alpha Bos taurus
2 Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA. Disulfides lactalbumin alpha Bos taurus
3 Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA. Disulfides lactalbumin alpha Bos taurus
4 Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA. Disulfides lactalbumin alpha Bos taurus
5 This X-alphaLA 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). Disulfides lactalbumin alpha Bos taurus
6 This X-alphaLA 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). Disulfides lactalbumin alpha Bos taurus
7 MD simulations have been used to characterize the X-alphaLA isomer and its formation via disulfide bond shuffling and to compare it with the native fold of alphaLA. Disulfides lactalbumin alpha Bos taurus
8 Calcium binding to native alphaLA is shown to help preserve the structure of the beta-domain of the protein limiting possibilities for disulfide bond shuffling. Disulfides lactalbumin alpha Bos taurus