TABLE 1.

Equilibrium properties of spectrin domains in the proteins discussed

Protein	ΔGD-N (kcal mol−1)	ΔΔGD-N (kcal mol−1)
R16 domain
R16 WT	6.1*	–
R16 in R1617 (R17 unfolded)	6.9*	−0.8*
R16 in R164I274	6.9	−0.8
R16 in R16-I27	7.0	−0.9
R16 in I27-R16	6.1	0.0
R16 in R1617A	7.0*	−0.9
R16 L97A	2.4†	–
R16 in R1617 L97A (R17 folded)	5.6‡	−3.2
R16 in R16-(Pro)3-R17	6.1‡	0.0
R17 domain
R17 WT	5.7*	–
R17 in R1617 (R16 folded)	7.5*	−2.8*
R17 in R174I274	6.8	−1.1
R17 in R17-I27	6.7	−1.0
R17 in I27-R17	5.7	0.0
16CR17	5.4*	0.4
R17 in R1617 L97A (R16 unfolded)	5.7‡	0.0

The error in ΔG_D-N is ±0.1 kcal mol⁻¹. The error in ΔΔG_D-N is ±0.2 kcal mol⁻¹.

^*Data are taken from Batey et al. (5).

^†Data are taken from Scott et al. (21).

^‡Data were determined using kinetic folding and unfolding rate constants, not equilibrium measurements.