Table 1.

Thermodynamic parameters for β1 parallel variants determined by chemical and thermal denaturation

Protein	Tm unfolding, K	Unf. transition range, K	ΔGunf., cal/mol K	Cm
WT	360	343 K –>373	3,857  ± 210	4.6
I6T53	345	333–363	4,697  ± 533	3.6
A6Y53	334	313–343	2,661  ± 109	1.5
A6F53	331	313–343	1,965  ± 203	2.0
F6A53	328	313–343	3,198  ± 142	1.7
A6A53	319	298–338	1,306  ± 647	1.5
F6G53	318	298–338	1,860  ± 366	1.1
G6Y53	318	298–338	1,362  ± 389	1.6

The variants are listed in decreasing order of melting temperatures. Thermal denaturations were performed in 50 mM sodium acetate buffer, pH 5.2. Protein concentrations ranged from 10 μM to 50 μM. Chemical denaturations were performed with GuHCl at 277 K in 50 mM sodium acetate buffer, pH 5.2. Protein concentrations ranged from 10 μM to 50 μM.