Converting trypsin to chymotrypsin: the role of surface loops.

By Lizbeth Hedstrom, L. Szilágyi, William J. Rutter. 1992

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Comparison of anionic and cationic trypsinogens: The anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structure (2008, methodology): “The mutant was constructed and purified as described previously~Hedstrom et al., 1992; Pasternak et al, 1998!. Circular dichroism spectra of trypsin and trypsinogen mutants: All spectra were measured using a Jovin-Yvon Mark V autodichrograph.”
Evolutionarily conserved networks of residues mediate allosteric communication in proteins (2003, unknown): “Substrate recognition in the chymotrypsin family of serine protease”
Highly active and selective endopeptidases with programmed substrate specificities. (2008, background): “Although the utility of structure-guided mutagenesis to swap substrate preferences between homologous proteases has been previously demonstrated8,9, the systematic engineering of protease specificity to accommodate a diverse set of substrate sequences while maintaining high catalytic activity has…”