Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant.

By L. Hedstrom, J. Perona, W. Rutter. 1994

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Protein sectors: evolutionary units of three-dimensional structure (2009, methodology): “…a standard chromophore-based assay on a model trypsin 778 Cell 138, 774–786, August 21, 2009 ª2009 Elsevier Inc. substrate peptide (NH2-AAPK-pNA) (Hedstrom et al., 1994), and stability by following the denaturation temperature (Tm) using the fluorescence of buried tryptophan residues as a…”
Molecular and Cellular Biophysics: Index (2006, background): “X–aminomethylcoumarin, with X either tryptophan or lysine as indicated (from Hedstrom et al., 1994).”
Evolutionarily conserved networks of residues mediate allosteric communication in proteins (2003, unknown): “However, appreciable exchange of trypsin specificity to that of chymotrypsin requires not only mutation of position 189 and the entire S1 pocket, but also substitution of an unexpectedly distributed group of residues comprising three surface loops (L1, L2 and L3”