Studies of the Aromatic Circular Dichroism of Staphylococcal Nuclease Binding Sites Circular Dichroism Deoxyribonucleases Ribonucleases In this article, Anfinsen, Omenn, and Cuatrecasas described the circular dichroism spectra of nuclease and of performic acid-oxidized derivative. Their findings suggested that the binding of the nucleotide inhibitor altered the asymmetric environment of certain tyrosyl residues. Furthermore, through titration, a method which can determine a substance or component in a solution by the addition of a liquid reagent of a known strength until a given endpoint, they were subsequently able to determine with greater certainty several of the amino acids present in the amino chain for staphylococcal nuclease. National Academy Press (U.S.), November 1969 National Academy Press, November 1969 Proceedings of the National Academy of Sciences of the United States of America Omenn, Gilbert S. Cuatrecasas, Pedro Anfinsen, Christian B. Anfinsen, Christian B. Articles Archival Materials Text 8 pages nlm:nlmuid-101584571X174-doc 101584571X174 http://resource.nlm.nih.gov/101584571X174 Profiles ID: KKBBLJ English Profiles in Science