Nuclear magnetic resonance study of a hybrid of bovine and rat ribonuclease.
A hybrid RNase S', consisting of synthetic S-peptide of rat ribonuclease and bovine S-protein, was studied by 1H n.m.r. to determine the effects of the many N-terminal amino acid replacements in rat S-peptide as compared to bovine S-peptide. As judged from the aromatic resonances, the conformation of the hybrid RNase S' is essentially identical to the conformation of bovine RNase S'. Notably, the active-site histidines 12 and 119 were not affected by the substitutions in the S-peptide, confirming earlier findings that the catalytic properties of naturally occurring RNases are modulated by the S-protein part of the molecule only. However, the resonances of Tyr-25 and His-48, which in RNase A are involved in a pH-dependent conformational transition, appeared to be different in the hybrid RNase, demonstrating that amino acid replacements may influence the structure of the protein locally.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D006639:Histidine / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D051381:Rats; D012260:Ribonucleases / Q000032:analysis* / Q000138:chemical synthesis; D014443:Tyrosine / Q000032:analysis
D014443:Tyrosine; D006639:Histidine; D012260:Ribonucleases