| Abstract | We found that the conserved motif stabilizes the cysteinate by hydrogen bonding to several NH backbone moieties. |
| Protein structure selection, search parameters and Cys environment characterization | Standard protonation states were assigned to all other titrable residues, D and Q were negatively charged, K and R positively charged and Histidine protonation was assigned favoring formation of hydrogen bonds in the crystal structure, but in the case of the already mentioned Histidine 214. |
| Results | However, we could not identify any over represented aminoacid (or aminoacid type) or any conserved set of interactions, not even Histidine, a residue that was proposed to form a hydrogen bond with the carbonyl group of the cysteine peptide bond in PTP 1B and relevant for Cys reactivity. |
| Results | The unusually low value seems to be the result of several strong hydrogen bond interactions that the deprotonated Cys performs with the protein environment (Shown in S7 Fig). |
| Results | Since potential SOH to backbone amide interaction could stabilize the constrained conformation, we analyzed the likelihood of internal hydrogen bond interactions between the amide hydrogen and either the sulfenic acid S or O atoms. |