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. [electronic resource]

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. [electronic resource] — المؤلف: Brown, L R — Jul 1978

المؤلف
Brown, L R
النشر
Jul 1978
الوصف
87-95 p.
الموضوعات
Alanine؛ Amides؛ Amines؛ Aprotinin؛ Arginine؛ Hydrogen-Ion Concentration؛ Magnetic Resonance Spectroscopy؛ Protein Conformation