Studies of the aromatic circular dichroism of Staphylococcal nuclease.

Proceedings of the National Academy of Sciences of the United States of America

PubMedID: 4984384

Omenn GS, Cuatrecasas P, Anfinsen CB. Studies of the aromatic circular dichroism of Staphylococcal nuclease. Proc Natl Acad Sci USA. 1969;64(3):923-30.
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.