Table 1. Correlation coefficients between VSD and PD voltage dependence–related fitted and calculated parameters and AA scales.
Scale type and code | L358X | L361X | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
V0 | V1 | V1/2 | E0 | E1 | S | V0 | V1 | V1/2 | E0 | E1 | S | ||
Hydrophobicity scales | |||||||||||||
GESa | 0.78 | 0.78 | 0.72 | 0.80 | -0.19 | -0.69 | 0.81 | 0.66 | 0.59 | 0.63 | 0.34 | -0.22 | |
HHb | 0.73 | 0.81 | 0.74 | 0.71 | -0.14 | -0.63 | 0.78 | 0.59 | 0.56 | 0.66 | 0.32 | -0.28 | |
KDc | 0.69 | 0.69 | 0.63 | 0.70 | -0.25 | -0.67 | 0.81 | 0.72 | 0.70 | 0.70 | 0.49 | -0.07 | |
MCd | 0.73 | 0.81 | 0.74 | 0.74 | -0.10 | -0.63 | 0.77 | 0.57 | 0.53 | 0.54 | 0.27 | -0.21 | |
MFe | 0.66 | 0.71 | 0.76 | 0.75 | -0.27 | -0.76 | 0.94 | 0.63 | 0.53 | 0.70 | 0.41 | -0.23 | |
WHPf | 0.73 | 0.54 | 0.44 | 0.63 | -0.48 | -0.75 | 0.79 | 0.85 | 0.80 | 0.62 | 0.62 | 0.04 | |
WWg | 0.81 | 0.92 | 0.78 | 0.75 | 0.08 | -0.55 | 0.63 | 0.41 | 0.34 | 0.45 | 0.09 | -0.38 | |
Size scales | |||||||||||||
ASAh | -0.7 | -0.67 | -0.66 | -0.70 | 0.29 | 0.71 | -0.88 | -0.76 | -0.74 | -0.65 | -0.5 | 0.03 | |
Lengthi | -0.17 | 0.05 | 0.09 | -0.10 | 0.36 | 0.32 | -0.27 | -0.80 | -0.82 | -0.25 | -0.82 | -0.65 | |
Widthj | 0.07 | 0.38 | 0.31 | 0.16 | 0.45 | 0.10 | -0.05 | -0.58 | -0.71 | -0.28 | -0.78 | -0.65 | |
Volumek | 0.15 | 0.46 | 0.37 | 0.20 | 0.36 | 0.05 | 0.02 | -0.57 | -0.67 | -0.06 | -0.75 | -0.79 |
Spearman correlation coefficients (rS) were calculated between each set of 20 voltage-dependent parameters and the indicated AA scale. Values of rS ≥0.7 or ≤−0.7, denoting very strong correlation, are shown in bold.
Goldman-Engelman-Steitz transfer free energies water–oil for AA side chains in ahelical polypeptides (Engelman et al., 1986).
Hessa-Hejne ΔG scale derived from H-segments with the indicated AA placed in the middle of the 19-residue hydrophobic stretch (Hessa et al., 2005).
Kyte and Doolittle hydropathy index derived from water-vapor transfer ΔG and interior–exterior distribution of AA side chains previously determined (Kyte and Doolittle, 1982).
Miller-Chothya transfer ΔG between the protein surface and interior (Miller et al., 1987).
Moon-Fleming water-to-bilayer transfer ΔG for the AA side chain (Moon and Fleming, 2011).
Wolfenden hydration potential: transfer ΔG of the AA side chain only from vapor to water (Wolfenden et al., 1981).
Wimley-White transfer ΔG of peptide AcWL-X-LL (X = AA) from bilayer interface to water (Wimley and White, 1996).
Median values of total ASA, in angstroms squared, of whole residues in ahelical structures (Lins et al., 2003).
STERIMOL length of the side chain (Fauchère et al., 1988).
STERIMOL width of the side chain (Fauchère et al., 1988).
Van de Waals volume of the residue (Nölting, 1999).