Table 3.

Isothermal Equilibrium Denaturation Data for WT FGF-1 and Mutant Proteins in Crystallization Buffer

Protein	Cm (M)	m-value (kJ mol−1 M−1)	ΔG (kJ mol−1)	ΔΔGa (kJ mol−1)	ΔΔG (pred.)b (kJ mol−1)
WT FGF-1c	1.29 ± 0.01	20.3 ± 0.7	26.6 ± 0.9	–
Ala66Cys (ox)d	1.84 ± 0.01	16.6 ± 1.0	30.5 ± 1.9	−10.2
Cys16Sere				12.1
Cys117Alaf	1.32 ± 0.01	20.5 ± 0.3	27.0 ± 0.4	−0.6
Pro134Ala
Pro134Valg				−8.8
C16S/A66C/C117A (ox)	1.24 ± 0.01	13.0 ± 0.3	16.1 ± 0.3	0.8	1.3
C16S/A66C/C117A (red)	1.12 ± 0.01	16.6 ± 0.4	18.6 ± 0.3	3.1
C16S/A66C/C117A/P134A (ox)	1.39 ± 0.02	12.4 ± 0.2	17.2 ± 0.2	−1.6	N.D.
C16S/A66C/C117A/P134A (red)	1.26 ± 0.01	17.0 ± 0.4	21.4 ± 0.4	0.6
C16S/A66C/C117A/P134V (ox)	1.83 ± 0.01	13.9 ± 0.2	25.4 ± 0.5	−9.2	−7.5
C16S/A66C/C117A/P134V (red)	1.69 ± 0.01	17.2 ± 0.3	29.1 ± 0.3	−7.5

The single letter amino acid code is used in naming combination mutants.

^aΔΔG = (C_{m WT} − C_{m mut}) (m_WT + m_mut)/2.

^bCalculated from the sum of individual point mutations.

^cDubey et al.³⁹

^dLee and Blaber.²⁵

^eDetermined from differential scanning calorimetry in 20 mM N-(2-acetamido) iminodiacetic acid (ADA), 0.1 M NaCl, pH 6.6 (“ADA buffer”)/0.7M GuHCl buffer.²⁴

^fXia et al.²¹

^gDetermined in ADA buffer.²⁷