Studies of the aromatic circular dichroism of Staphylococcal nuclease.
Specific contributions of tyrosyl and of tryptophanyl residues can be distinguished in the near-ultraviolet circular dichroic spectrum of staphylococcal nuclease. Upon binding of the inhibitor deoxythymidine 3',5'-diphosphate in the presence of Ca(++), a significant change in the circular dichroic spectrum results which has been used to characterize the interaction of ligand and enzyme. The data suggest that the asymmetric environment of certain tyrosyl residues is altered by binding of the nucleotide inhibitor.
D001665:Binding Sites; D002118:Calcium; D003851:Deoxyribonucleases / Q000032:analysis* / Q000037:antagonists & inhibitors; D004492:Edetic Acid; D009711:Nucleotides; D012260:Ribonucleases / Q000032:analysis* / Q000037:antagonists & inhibitors; D013057:Spectrum Analysis; D013210:Staphylococcus / Q000201:enzymology*; D014443:Tyrosine
D009711:Nucleotides; D014443:Tyrosine; D004492:Edetic Acid; D003851:Deoxyribonucleases; D012260:Ribonucleases; D002118:Calcium