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. 1969 Nov;64(3):923–930. doi: 10.1073/pnas.64.3.923

STUDIES OF THE AROMATIC CIRCULAR DICHROISM OF STAPHYLOCOCCAL NUCLEASE

Gilbert S Omenn 1, Pedro Cuatrecasas 1, Christian B Anfinsen 1
PMCID: PMC223323  PMID: 4984384

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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