Nuclear Magnetic Resonance Studies of α-Chymotrypsin. I. NMR Studies of the Binding of Small Molecule Inhibitors to α-Chymotrypsin. II. NMR Studies of the Interaction of N-TFA-D-Tryptophan Semicarbazide with α-Chymotrypsin. III. ¹³C-NMR Studies of Methylated α-Chymotrypsin. IV. NMR Studies of Acylated Chymotrypsins
<p>Part I</p> <p>Magnetic resonance studies of the interaction of N-trifluoro-acetyl-D-(and L-)p-fluorophenylalanine and N-trifluoro-acetyl-D-(and L-)tryptophan with α-chymotrypsin have been carried out at pH 5.0-8.0. The effect of enzyme oligomerization and competitive inhib...
Internet
https://thesis.library.caltech.edu/10673/1/Gammon_kl_1973.pdfGammon, Kenneth Lee (1973) Nuclear Magnetic Resonance Studies of α-Chymotrypsin. I. NMR Studies of the Binding of Small Molecule Inhibitors to α-Chymotrypsin. II. NMR Studies of the Interaction of N-TFA-D-Tryptophan Semicarbazide with α-Chymotrypsin. III. ¹³C-NMR Studies of Methylated α-Chymotrypsin. IV. NMR Studies of Acylated Chymotrypsins. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/XXJX-AD69. https://resolver.caltech.edu/CaltechTHESIS:02052018-102944228 <https://resolver.caltech.edu/CaltechTHESIS:02052018-102944228>