Comparison of the (30-51, 14-38) Two-disulphide Folding Intermediates of the Homologous Proteins Dendrotoxin K and Bovine Pancreatic Trypsin Inhibitor by Two-dimensional1H Nuclear Magnetic Resonance
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Cited by 9 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. Oxidative Folding: Coupling Conformational Folding and Disulfide Formation;Folding of Disulfide Proteins;2011
2. Conformational Exchange Is Critical for the Productivity of an Oxidative Folding Intermediate with Buried Free Cysteines;Journal of Molecular Biology;2010-10
3. The NMR Structures of the Major Intermediates of the Two-domain Tick Carboxypeptidase Inhibitor Reveal Symmetry in Its Folding and Unfolding Pathways;Journal of Biological Chemistry;2008-10
4. Folding of small disulfide-rich proteins: clarifying the puzzle;Trends in Biochemical Sciences;2006-05
5. Conkunitzin-S1 Is the First Member of a New Kunitz-type Neurotoxin Family;Journal of Biological Chemistry;2005-06
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