Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1984.tb08572.x/fullpdf
Reference22 articles.
1. 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
2. Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolution
3. Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution
4. 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
5. The Influence of Localized Chemical Modifications of the Basic Pancreatic Trypsin Inhibitor on Static and Dynamic Aspects of the Molecular Conformation in Solution
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