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Table 3 Correlations between electronic properties and folding preferencesa.

From: Electronic properties of amino acid side chains: quantum mechanics calculation of substituent effects

Index HNNMR σI σR σα σF AI CαMULL
Kyte-Doolittle -0.8** 0 0 -0.2 0.3 -0.5* 0.4
Water vapor 0.8** 0.2 0.2 0.1 -0.6* 0.5* -0.4
Bulk -0.3 -0.1 -0.2 0.9** 0 0.2 -0.4
Gyration -0.2 0 -0.2 0.9** 0 0.3 -0.5*
α-helix -0.1 0.3 0.1 0.2 -0.2 0.6** -0.7**
β-strand -0.8** -0.2 -0.1 0.3 0.3 -0.4 0.2
coil 0.7** 0.1 0.4 -0.3 -0.4 0.3 -0.3
eσ -0.1 -0.9** -0.9** 0.3 0.7** -0.6** 0.4
pKa -0.1 0.3 0.3 -0.3 0.1 0 0
σI 0.2       
σR 0.2 0.8**      
σα -0.4 -0.1 -0.2     
σF -0.4 -0.8** -0.9** 0    
AI 0.5* 0.7** 0.5* 0 -0.6**   
CαMULL -0.2 -0.6* -0.4 -0.2 0.5* -0.8**  
  1. aLinear regression analysis was performed to determine possible correlations between the various electronic scales presented here. The first 2 indices of hydrophobicity were taken from Kyte and Doolittle [46], the bulk scale was from Kidera et al. [38], and the gyration scale is that of Levitt [39]. The secondary structure preferences and eσ scales were described previously [8]. The r values from the analysis are presented here and directions of the slope are indicated by the signs. Statistical analysis of the data revealed significant correlations: *p < 0.05, **p < 0.01.