The Amino Acid Sequence of an Extracellular Nuclease of Staphylococcus aureus: I. Linear Order of the Fragments Produced by Cleavage with Cyanogen Bromide

Throughout the late 1960s, the primary concern of Anfinsen's laboratory was to understand the relationship between structure and function in staphylococcal nuclease. Anfinsen chose to study this enzyme because it was relatively small, with only 149 amino acids, and because it appeared to be entirely dependent on noncovalent binding for the maintenance of an ordered catalytically active structure. In this series of three articles, authored by Anfinsen and Taniuchi, but based primarily on research conducted by the latter, the two scientists presented the first analysis of the primary sequence of the enzyme.