Table 2 Correlation of pH50 and pHD50 values with side chain properties

From: Molecular mechanisms and hotspots of pH sensing in ASIC1a revealed by computational and functional analysis

 

Residue

 

Activation

SSD

  

Number of mutations studied

positive correlation

Negative correlation

positive correlation

Negative correlation

Palm

H73

7

h_do (0.046)

 

pol (0.020), h_ac (0.026), coil (0.024)

hyd (0.032), bulk (0.038)

D78

7

pol (0.028), h_ac (0.004)

  

h_do (0.011)

H173

4

    

E277

4

    

K374

7

size (0.013), surf (0.005), h_do (0.029)

   

E375

5

 

h_do (0.013)

h_ac (0.005)

h_do (0.08)

E413

5

h_ac (0.012)

beta (0.01), h_do (0.015)

h_ac (0.001)

 

E418

4

pol (0.052)

  

coil (0.017)

Acidic pocket

K211

6

   

flex (0.011)

E219

4

    

E242

4

  

h_ac (0.016)

 

K246

7

   

h_ac (0.016)

Thumb

H329

7

    

Knuckle

K384

4

coil (0.031)

alpha (0.02), bulk (0.026)

  

K388

4

  

size (0.045)

 
  1. Correlations between different scales of amino acid side chain biophysical properties were determined as described in Methods and in Supplementary Data 1. The p value is indicated in parenthesis. Alpha, α helix propensity; beta, β-sheet propensity; bulk, bulkiness; coil, coil structure propensity; flex, flexibility; h_ac, H+ acceptor, h_do, H+ donor; hyd, hydropathy; pol, polarity; surf, surface.
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