The application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozyme.
We review our research on triose-phosphate isomerase and bacteriophage T4 lysozyme. In our studies over the last ten years we have used electrostatic potentials, computer graphics, quantum mechanics, molecular mechanics, molecular dynamics and free energy calculations to try to understand why triose-phosphate isomerase is such an efficient enzyme and why its efficiency is dramatically decreased by several site-specific mutations. For T4 lysozyme we have used free energy methods to analyse and try to understand why Thr-157----Val and Thr-157----Ala mutations decrease protein stability by about 1-2 kcal/mol.
Kollman
P A
PA
Department of Pharmaceutical Chemistry, UCSF 94143.
Daggett
V
V
Dang
L X
LX
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D004099:Dihydroxyacetone Phosphate / Q000378:metabolism; D008432:Mathematical Computing; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D009154:Mutation; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D013604:T-Phages / Q000201:enzymology; D014305:Triose-Phosphate Isomerase / Q000737:chemistry*
D004099:Dihydroxyacetone Phosphate; D009113:Muramidase; D014305:Triose-Phosphate Isomerase