The behavior of the active site salt bridge of bovine neurophysins as monitored by 15N NMR spectroscopy and chemical substitution. Relationship to biochemical properties

Biochemistry

Volumn 35, Issue 36, 1996, Pages 11763-11772

  Zheng, Changsheng ^a   Cahill, Scan ^b   Breslow, Esther ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GLUTAMIC ACID; LIGAND; NEUROPHYSIN;

ARTICLE; CATTLE; CHEMICAL MODIFICATION; DIMERIZATION; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTON NUCLEAR MAGNETIC RESONANCE;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATTLE; DIPEPTIDES; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; NEUROPHYSINS; OXYTOCIN; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; TRYPSIN;

EID: 0029786384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi960906a     Document Type: Article

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