Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. III. Mutual electrostatic interaction between histidine residues 12 and 119.
The two adjacent active site histidine residues of bovine pancreatic ribonuclease A (histidine-12 and -119) yield proton magnetic resonance titration curves having Hill coefficients significantly less than unity (0.7 and 0.8, respectively). Three models postulating interactions with other titrating groups in the molecule have been used to approximate these anomalous experimental titration curves. Very good agreement with the data was obtained with models postulating mutual electrostatic interaction between histidine-12 and -119. The additional low pH perturbation of the chemical shift of the C(2)-H peak (but not the C(4)-H peak) of histidine-12 is attributed to a local conformational change with a pHmid of about 3.5.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D006639:Histidine / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D010179:Pancreas / Q000201:enzymology; D011485:Protein Binding; D011487:Protein Conformation; D012260:Ribonucleases
D006639:Histidine; D012260:Ribonucleases