Unusually large electrostatic field effect of the buried aspartate in serine proteinases: Source of catalytic power

This publication has 24 references indexed in Scilit:

• Theoretical calculations on proton-transfer energetics: studies of methanol, imidazole, formic acid, and methaneethiol as models for the serine and cysteine proteases
  Journal of the American Chemical Society, 1981
• Simple calculation of electrostatic isopotential maps from bond fragments
  Journal of Computational Chemistry, 1981
• Neutron diffraction identifies His 57 as the catalytic base in trypsin
  Nature, 1980
• Electrostatic isopotential maps for large biomolecules
  International Journal of Quantum Chemistry, 1979
• A Comparison of the Energetics of Proton Transfer in the Serine and Cysteine “Charge Relay” Systems and the Role of the Protein Electrostatic Potential on the Proton Transfer Energetics
  Published by Springer Nature ,1979
• 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
• Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin A.alpha.
  Biochemistry, 1978
• Serine Proteases: Structure and Mechanism of Catalysis
  Annual Review of Biochemistry, 1977
• THE NATURE OF GENERAL BASE-GENERAL ACID CATALYSIS IN SERINE PROTEASES
  Proceedings of the National Academy of Sciences, 1969
• Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin
  Nature, 1969