Table 2. Force field parameters for carbonylated amino acids.

Here, ${\epsilon }_{\mathrm{G}\mathrm{h}\mathrm{a}\mathrm{v}\mathrm{a}\mathrm{m}\mathrm{i}}$ and ${\epsilon }_{\mathrm{n}\mathrm{a}\mathrm{t}\mathrm{i}\mathrm{v}\mathrm{e}}$ represent the hydrophobicity of amino acids in their native condition according to Ghavami et al. (2014) and the weighted average scheme, respectively. ${\epsilon }_{\mathrm{c}\mathrm{a}\mathrm{r}\mathrm{b}\mathrm{o}\mathrm{n}\mathrm{y}\mathrm{l}\mathrm{a}\mathrm{t}\mathrm{e}\mathrm{d}}$ denotes the hydrophobicity derived from the weighted average scheme and $q_{\mathrm{n}\mathrm{a}\mathrm{t}\mathrm{i}\mathrm{v}\mathrm{e}\mathrm{}\mathrm{t}\mathrm{o}\mathrm{}\mathrm{c}\mathrm{a}\mathrm{r}\mathrm{b}\mathrm{o}\mathrm{n}\mathrm{y}\mathrm{l}\mathrm{a}\mathrm{t}\mathrm{e}\mathrm{d}}$ stands for the charge modification from the native to the carbonylated state.

AA	${\mathit{\epsilon }}_{\mathbf{G}\mathbf{h}\mathbf{a}\mathbf{v}\mathbf{a}\mathbf{m}\mathbf{i}}$	${\mathit{\epsilon }}_{\mathbf{n}\mathbf{a}\mathbf{t}\mathbf{i}\mathbf{v}\mathbf{e}}$	${\mathit{\epsilon }}_{\mathbf{c}\mathbf{a}\mathbf{r}\mathbf{b}\mathbf{o}\mathbf{n}\mathbf{y}\mathbf{l}\mathbf{a}\mathbf{t}\mathbf{e}\mathbf{d}}$	${\mathit{q}}_{\mathbf{n}\mathbf{a}\mathbf{t}\mathbf{i}\mathbf{v}\mathbf{e}\mathbf{}\mathbf{t}\mathbf{o}\mathbf{}\mathbf{c}\mathbf{a}\mathbf{r}\mathbf{b}\mathbf{o}\mathbf{n}\mathbf{y}\mathbf{l}\mathbf{a}\mathbf{t}\mathbf{e}\mathbf{d}}$
T	0.51	0.52	0.34	0 −>0
K	0.00	0.00	0.59	1 −>0
P	0.65	0.63	0.43	0 −>0
R	0.00	0.07	0.43	1 −>0