High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. I. The hydrogen bonded protons of the "charge relay" system.

[1]  R. Shulman,et al.  High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors. , 1974, Journal of molecular biology.

[2]  M. Hunkapiller,et al.  Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases. , 1973, Biochemistry.

[3]  J. Beintema,et al.  Proton nuclear magnetic resonance studies of histidine residues in rat and other rodent pancreatic ribonucleases. Effects of pH and inhibitors. , 1973, Journal of molecular biology.

[4]  A. Schechter,et al.  The assignment of an exchangeable low-field NH proton resonance of ribonuclease A to the active-site histidine-119. , 1973, Biochemistry.

[5]  R. Shulman,et al.  Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome c. , 1973, Journal of molecular biology.

[6]  R. Shulman,et al.  High resolution nuclear magnetic resonance study of the histidine--aspartate hydrogen bond in chymotrypsin and chymotrypsinogen. , 1972, Journal of molecular biology.

[7]  A. Fersht,et al.  Conformational equilibria in -and -chymotrypsin. The energetics and importance of the salt bridge. , 1972, Journal of molecular biology.

[8]  C. Yim,et al.  Studies of the histidine residues of carbonic anhydrases using high-field proton magnetic resonance. , 1972, Biochemistry.

[9]  D. Blow,et al.  Structure of crystalline methyl-chymotrypsin. , 1972, Journal of molecular biology.

[10]  T. Horbett,et al.  Reevaluation of the activation of bovine chymotrypsinogen A. , 1971, Biochemistry.

[11]  R. Shulman,et al.  High resolution nuclear magnetic resonance study of base pairing in four purified transfer RNA molecules. , 1971, Journal of molecular biology.

[12]  G. Cohen,et al.  Substrate binding site in bovine chymotrypsin A-gamma. A crystallographic study using peptide chloromethyl ketones as site-specific inhibitors. , 1971, Biochemistry.

[13]  G. Roberts,et al.  Nuclear magnetic resonance studies of human carbonic anhydrase B. Histidine residues. , 1971, Biochemistry.

[14]  R. Shulman,et al.  Nuclear magnetic resonance study of cyanoferrimyoglobin; identification of pseudocontact shifts. , 1970, Journal of molecular biology.

[15]  D. Shotton,et al.  Three-dimensional Structure of Tosyl-elastase , 1970, Nature.

[16]  D. Shotton,et al.  Three-dimensional Fourier Synthesis of Tosyl-elastase at 3.5 Å Resolution , 1970, Nature.

[17]  G. P. Hess,et al.  Studies of the activity of chymotrypsin. , 1970, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[18]  E. Kaiser,et al.  [1] Principles of active site titration of proteolytic enzymes , 1970 .

[19]  P. E. Wilcox.  [5] Chymotrypsinogens—chymotrypsins , 1970 .

[20]  G. Fasman,et al.  Conformation of the high pH form of chymotrypsin. , 1969, Journal of molecular biology.

[21]  D. Blow,et al.  Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin , 1969, Nature.

[22]  J. Kraut,et al.  Structure of Subtilisin BPN′ at 2.5 Å Resolution , 1969, Nature.

[23]  W. Jencks.  Catalysis in chemistry and enzymology , 1969 .

[24]  G. Czerlinski,et al.  Conformation and Activity of Chymotrypsin: The pH-Dependent, Substrate-Induced Proton Uptake , 1968, Science.

[25]  B. Matthews,et al.  Structure of crystalline -chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism. , 1968, Journal of molecular biology.

[26]  G. P. Hess,et al.  Conformational changes accompanying the formation of chymotrypsin-substrate complexes. Evidence for the involvement of an N-terminal alpha-amino group in the activity and the conformation of the enzyme. , 1964, Biochemical and Biophysical Research Communications - BBRC.

[27]  Manfred Eigen,et al.  Proton Transfer, Acid-Base Catalysis, and Enzymatic Hydrolysis. Part I: ELEMENTARY PROCESSES†‡ , 1964 .

[28]  E. Shaw,et al.  Direct evidence for the presence of histidine in the active center of chymotrypsin. , 1963, Biochemistry.

[29]  G. Hammes,et al.  FAST REACTIONS OF IMIDAZOLE STUDIED WITH RELAXATION SPECTROMETRY , 1960 .