Table 4.

Summary of molecular cooperativity in Trx characterized by identifying correlated regions for T=338 K

Reference residue(s)	Flexibly correlated	Rigidly correlated	Uncorrelated
Active site Cys32, Gly33, Pro34, Cys35	None, the active site is always a rigid unit	Except for uncorrelated regions, the entire protein is rigidly correlated	7–22, 62–76, 92–108
Side flanks to the active site at residues Trp31 or Met37 giving virtually identical results	61–75, 92–95, 105	None. The flanking sides of the active site are always flexible	7–22, 96–104, 106–108
Gln50	This location is rigid, and therefore is not flexibly correlated with any region	Weakly to 7–18 and more strongly to 33, 35 which are in the active site	19–23, 62–76, 92–108
Arg73	1–22, 26–32, 37–39, 48–54, 58–77, 91–95 Both flanking sides to the active site are included	Virtually none, except weak correlation to the helix between 40–44	Everything else