Characterization of an alternative low energy fold for bovine α-lactalbumin formed by disulfide bond shuffling
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.23247/fullpdf
Reference42 articles.
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4. Protein disulfide-isomerase-building bridges in protein-folding;Freedman;Trends Biochem Sci,1994
5. Pathways for protein disulphide bond formation;Frand;Trends Cell Biol,2000
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Effects of Metal Ions, Temperature, and a Denaturant on the Oxidative Folding Pathways of Bovine α-Lactalbumin;International Journal of Molecular Sciences;2017-09-16
2. Accessibility explains preferred thiol-disulfide isomerization in a protein domain;Scientific Reports;2017-08-29
3. Characterization of the flexible lip regions in bacteriophage lambda lysozyme using MD simulations;European Biophysics Journal;2015-03-28
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