Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor. Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1984.tb08571.x/fullpdf
Reference35 articles.
1. The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor. 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
2. The Influence of Localized Chemical Modifications of the Basic Pancreatic Trypsin Inhibitor on Static and Dynamic Aspects of the Molecular Conformation in Solution
3. Conformational Studies by 1H Nuclear Magnetic Resonance of the Basic Pancreatic Trypsin Inhibitor after Reduction of the Disulfide Bond between Cys-14 and Cys-38. Influence of Charged Protecting Groups on the Stability of the Protein
4. Dynamic model of globular protein conformations based on NMR studies in solution
5. Correlations between internal mobility and stability of globular proteins
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