Table 1.

Stabilities of DHFR_Mp variants fused to eGFP in bulk solution and in the GroE and thermosome cavities

Protein*	Exposed surface area of mutated residue in the native state (Å2)†	Percent area of mutated residue exposed in the native state†	Stability in bulk solution (kcal mol−1)	Change in stability in bulk solution upon mutation (kcal mol−1)‡	Stability in the cavity (kcal mol−1)	Change in stability in the cavity upon mutation (kcal mol−1)‡
WT in GroE§	-	-	−3.45 ± 0.09	-	2.4 ± 0.2	-
WT in (αβ)4	-	-	−3.45 ± 0.09	-	2.7 ± 0.3	-
WT in β9	-	-	−3.45 ± 0.09	-	3.3 ± 0.2	-
L9V in GroE	4.0	3.5	−2.60 ± 0.13	0.85 ± 0.15	3.7 ± 0.3	1.3 ± 0.4
I41V in GroE	0.0	0	−2.95 ± 0.07	0.50 ± 0.11	1.6 ± 0.1	−0.8 ± 0.2
I61V in GroE	0.1	0	−3.16 ± 0.07	0.29 ± 0.11	2.2 ± 0.2	−0.2 ± 0.3
L93V in GroE	5.4	4.0	−1.52 ± 0.18	1.93 ± 0.20	0.9 ± 0.1	−1.5 ± 0.2
I95V in GroE	5.8	3.5	−3.03 ± 0.09	0.42 ± 0.13	2.8 ± 0.3	0.4 ± 0.4

^*Single-letter notation of amino acids is used.

^†Values represent averages for the two dihydrofolate reductase chains (A and B) related by noncrystallographic symmetry in the crystal structure (PDB ID: 2zza). The solvent-accessible surface areas for each residue listed were calculated using PyMOL.

^‡The changes in stability in bulk solution and in the cavity upon mutation were calculated as: ∆G(mutant) – ∆G(wild-type).

^§The data for wild-type DHFR_Mp in the chimera were reported before (23).