Role of Asp102 in the enzymatic reaction of bovine β-trypsin

This publication has 31 references indexed in Scilit:

• A molecular orbital study on the zinc-water-Glu 270 system in carboxypeptidase A.
  CHEMICAL & PHARMACEUTICAL BULLETIN, 1981
• Effects of the hydrogen bond between His 57 and Asp 102 on the lone pair molecular orbital of nitrogen of His 57 in serine proteases.
  CHEMICAL & PHARMACEUTICAL BULLETIN, 1980
• The molecular orbital study on the role of hydrogen bonding system in the active site of serine proteases.
  CHEMICAL & PHARMACEUTICAL BULLETIN, 1980
• Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases
  Journal of the American Chemical Society, 1978
• Ab initio molecular orbital studies on the aspirin solvolysis and ester hydrolysis.
  CHEMICAL & PHARMACEUTICAL BULLETIN, 1977
• A molecular orbital theoretical study on the acid-base property and reactivity of the charge relay system in α-chymotrypsin
  Journal of Theoretical Biology, 1976
• Theoretical calculations on an acetic acid, 5-methylimidazole, methanol hydrogen bond network: A model charge relay system
  Journal of Theoretical Biology, 1974
• High resolution nuclear magnetic resonance studies of the active site of chymotrypsin: I. The hydrogen bonded protons of the “charge relay” system
  Journal of Molecular Biology, 1974
• A molecular orbital study on the enzymic reaction mechanism of α-chymotrypsm
  Journal of Theoretical Biology, 1973
• Atomic coordinates for subtilisin BPN′ (or Novo)
  Biochemical and Biophysical Research Communications, 1971