Design of stable circular permutants of the GroEL chaperone apical domain

Table 1 Heat denaturation parameters for the AD-GroEL protein and circular permutants obtained by different methods

	PONDR	DSC t_m, C (± 0.1)	CD Θ₂₁₀ t_1/2,C (± 0.3)	CD Θ₂₂₀ t_1/2,C (± 0.3)
wt	0.03	71.1	73.8	72.4
cp211	0.31	66.2	66.4	64.3
cp244	0.40	54.9	54.5	60.4
cp256	0.66	—	57.6	55.6
cp269	0.23	65.5	56.6	55.5
cp282	0.38	61.1	63.4	62.7
cp297	0.69	45.1 and 51	59.2	59.8

PONDR—Intrinsic disorder score of specified amino acid residues predicted by PONDR® VLXT program
DSC t_m—the maximum temperatures of the heat absorption peaks of protein obtained by the DSC method
CD Θ₂₁₀ t_1/2—the half-transition temperatures obtained by the CD ellipticity at 210 nm
CD Θ₂₂₀ t_1/2—the half-transition temperatures obtained by the CD ellipticity at 220 nm

ISSN: 1478-811X