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. Author manuscript; available in PMC: 2014 Jul 31.
Published in final edited form as: J Am Chem Soc. 2013 Jul 18;135(30):11181–11192. doi: 10.1021/ja403917z

Table 2.

MD electrostatic data for C=O bonds in solvents and proteins

|Fvib| / (MV/cm) a |ΔFvib| / (MV/cm) b
mean std. dev. mean std. dev.
hexanes −0.115 0.77 −0.029 0.76
dibutylether −7.40 6.42 −0.28 3.83
chloroform −28.5 13.6 −13.7 12.7
tetrahydrofuran −15.5 9.36 −0.19 6.09
dichloromethane −25.5 15.9 −8.66 11.6
valeronenitrile −19.2 12.0 −0.67 7.46
acetonitrile −25.3 13.6 −3.73 9.58
dimethylsulfoxide −29.6 11.5 −1.53 10.1
water (TIP3P) −65.9 23.1 −40.7 25.7
[p-Ac-Phe]S-peptide −63.6 [−61.9]c 39.6 [39.0] c −38.1 [–38.6] c 33.1 [33.3] c
[p-Ac-Phe]RNase S −13.4 [−11.5] c 7.05 [7.00] c −3.44 [−4.00] c 4.90 [5.04] c
a

The electric field experienced by the C=O vibration, as defined by Eq. 4.

b

The electric field drop across the C=O vibration, as defined by Eq. 5.

c

For the bottom two entries, the set of values in brackets reflect calculations that do count the probe-bearing residue’s backbone atoms as part of the environment (see text).