Showing papers by "Joseph S. Fruton published in 1974"
TL;DR: Steady state fluorescence measurements showed that neither active papain nor papain inactivated by blockage of the active site sulfhydryl group has appreciable intrinsic affinity for the mansyl group, but that themansyl group of compounds such as Mns-Gly-Val-Glu-Leu-Gy is drawn, by peptide-protein interaction, into an environment of lower dynamic polarity.
32 citations
TL;DR: Studies on the kinetics of the cleavage of oligopeptide substrates by pepsin, together with the examination of the changes in fluorescence of dansyl or mansyl peptides upon interaction with pepsInogen, give further evidence of the importance of secondary interactions of such substrates with the extended active site of the enzyme.
Abstract: Studies on the kinetics of the cleavage of oligopeptide substrates by pepsin, together with the examination of the changes in fluorescence of dansyl or mansyl peptides upon interaction with pepsin or pepsinogen, give further evidence of the importance of secondary interactions of such substrates with the extended active site of the enzyme and indicate considerable conformational flexibility at the active site of pepsin in response to enzyme–substrate interaction.
3 citations
TL;DR: The absorption and emission spectra of these acyl-aminoacridines are not altered by interaction with DNA to the extent seen with the 9-amINOacridinium cation under comparable experimental conditions.
3 citations