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Table 2 Propensity of polar residues forming sidechain hydrogen bonds to mainchain atoms in various architectural contexts.

From: On the evolutionary conservation of hydrogen bonds made by buried polar amino acids: the hidden joists, braces and trusses of protein architecture

  Propensity of polar residues forming sidechain hydrogen bonds to mainchain atoms
Amino Acid Within helix N-termini Within helix C-termini Within edge strands From edge strands Within central strands From central strands Within 310 helices Within β-hairpins Within polyproline helices Within coil regions
  Con All Con All Con All Con All Con All Con All Con All Con All Con All Con All
Arg 1.05 0.46 14.38 6.44 3.17 3.29 1.71 3.25 0.34 1.73 3.07 3.42 3.02 3.52 1.48 2.69 6.11 3.70 2.48 3.52
Asn 1.30 2.88 1.14 1.84 3.12 3.20 3.20 2.00 2.44 2.44 3.06 2.30 1.58 2.41 1.13 3.05 2.54 2.43 1.85 2.57
Asp 4.84 3.04 0.61 0.54 2.65 1.20 2.27 2.06 0.97 1.44 2.42 1.46 3.04 2.28 6.37 2.97 1.74 1.43 5.20 2.52
Cys 9.86 2.20 4.52 1.40 3.83 2.66 0.93 2.22 5.09 4.06 0.39 2.53 8.99 2.59 4.51 1.70 1.55 0.84 5.94 1.97
Gln 0.11 1.22 0.44 1.80 2.33 2.98 6.19 2.23 4.87 1.86 1.67 2.10 0.96 1.69 1.04 1.80 1.55 3.06 0.52 1.96
Glu 1.94 1.40 0.00 0.06 0.00 0.82 0.00 0.64 0.57 0.48 2.35 0.78 0.81 0.79 0.08 0.93 0.80 1.19 0.90 0.99
His 2.37 1.13 0.89 2.50 0.97 2.24 4.08 2.14 0.82 2.08 1.81 2.22 1.45 2.62 1.90 1.89 4.71 2.38 2.66 2.08
Lys 0.00 0.13 0.60 1.99 0.00 1.05 0.00 0.88 1.25 0.51 0.00 1.12 0.15 1.18 0.00 0.67 0.40 1.00 0.13 0.97
Ser 1.53 3.43 0.65 2.15 0.47 1.92 2.61 2.01 2.32 3.22 2.46 1.75 1.09 2.01 3.58 2.23 0.76 2.03 0.90 1.95
Thr 1.53 3.64 0.70 2.05 2.91 1.81 0.68 2.25 3.43 3.29 0.48 2.37 0.65 1.88 0.75 2.23 0.62 1.88 1.19 1.81
Trp 0.81 0.23 0.36 1.28 2.06 1.31 6.53 2.01 1.84 1.83 1.84 1.83 3.41 1.23 3.88 1.40 2.93 1.25 3.58 1.30
Tyr 1.06 0.68 0.56 1.23 4.04 1.77 0.30 2.37 1.03 1.26 3.14 2.37 4.20 1.37 0.07 0.91 3.12 1.84 1.60 1.39
  1. Columns headed "Col" display the propensities of conserved buried polar residues.
  2. Columns headed "All" display the propensities of all polar residues forming the indicated interaction (regardless of solvent accessibility or conservation).