Fig. 2.

Systematic variation of protein surface flexibility and its effects on thermodynamic activation parameters. (A) Simulation sphere where solute atoms between R_shell (18, 20, 22, 24, 26, and 30 Å) and 35 Å are restrained with a force constant of 100 kcal/(mol⋅Ų). (B) Thermodynamic activation parameters (300 K) for the systems restrained in A, showing that the parameters for cold-active trypsin are gradually converted to those of the warm-adapted trypsin. See Table S1 for the number of solute atoms in each restrained shell.