Table 1.

ΔΔG°′_D→M values at 298 K predicted by scaled particle theory (SPT) and calculated from NMR data (pH 7.5) for the domain-swapped (L = 0.5) and side-by-side dimer (L = 0.7)

		ΔΔG°′D→M, kcal/mol*
		Domain-swapped		Side-by-side
Cosolute	g/L	SPT†	NMR‡	SPT†	NMR‡,§
Sucrose	300	1.38	0.26 ± 0.06	0.67	0.03 ± 0.04
Ethylene glycol	200	1.50	−0.30 ± 0.06	0.76	−0.29 ± 0.05
TMAO	38	0.25	0.16 ± 0.06	0.13	0.50 ± 0.06
Urea	100	0.61	−1.31 ± 0.05	0.31	−0.25 ± 0.04
BSA	100	0.14	0.51 ± 0.05	0.10	0.48 ± 0.06
Lysozyme	50	0.09	−0.12 ± 0.05	0.05	−0.18 ± 0.05
Ficoll-70	300	N/A¶	0.71 ± 0.06	N/A¶	0.15 ± 0.04
8-kDa PEG	200	N/A¶	0.39 ± 0.06	N/A¶	−0.22 ± 0.03

^*Positive values indicate increased dimer stability.

^†As described by Berg (12) using parameters from SI Appendix, Table S1.

^‡Uncertainties are the SD of the mean from triplicate analysis.

^§From Guseman and Pielak (37).

^¶Ficoll and PEG cannot be simulated with scaled particle theory at these concentrations.