Table 2.

Thermodynamics of the binding-coupled folding of TRAP

Change in Solvent Accessible Surface Area (ΔASA):
Absence of folding a
Polar	239 Å2
Nonpolar	378 Å2
Presence of folding b
Polar	1328 Å2
Nonpolar	1916 Å2
Change in Heat Capacity (ΔCp):
Expected from tryptophan burial c	-88 cal mol-1 K-1
Experimental	-370 cal mol-1 K-1
Upper limit for folding d	-427 cal mol-1 K-1
Binding-Coupled Folding (ℜ):
ITC	17-24 residues/monomer
NMR e	19 residues/monomer

^aΔASA for the burial of tryptophan measured from the structure 1QAW (14); see methods.

^bΔASA for the burial of tryptophan and the 19 residues that exhibit ligand-dependent line broadening, measured from the structure 1QAW (14); see methods.

^cExpected heat capacity change in the absence of folding calculated from ΔASA ^a using equation 1.

^dUpper limit for the heat capacity change in the presence of folding if all the residues go from an extended structure to a folded structure calculated from ΔASA ^b using equation 1.

^eNumber of residues for which the NMR resonances are exchange-broadened beyond detection in apo-TRAP but are present in holo-TRAP and are located in the tryptophan or RNA-binding sites.