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International Journal of Biological Macromolecules|April 1, 1991
Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pHM M Dixon, R G Brennan, B W Matthews
Biopolymers|November 1, 1992
Flexible-geometry conformational energy maps for the amino acid residue preceding a prolineJ H Hurley, D A Mason, B W Matthews
Protein Science : a Publication of the Protein Society|June 1, 1992
Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stabilityX J Zhang, W A Baase, B W Matthews
European Journal of Biochemistry|June 2, 1986
Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysinD E Tronrud, A F Monzingo, B W Matthews
The Journal of Biological Chemistry|October 5, 2001
The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPaseA C Hausrath, R A Capaldi, B W Matthews
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