Fig. 3: Amino acid selectivity of electrophiles targeting cysteines.
From: Profiling the proteome-wide selectivity of diverse electrophiles
a–c,e,f, Structures of alkyne probes containing α-halocarbonyl (a), SNAr (b), hypervalent iodine (c), SN2 (e) or Michael acceptor (f) electrophiles that were investigated for their proteome-wide amino acid selectivity. Orange circles indicate the initial site of electrophilic reactivity. d,g, Amino acid selectivity of probes targeting cysteines (d) and reacting as Michael acceptors (g) upon treatment of the proteome of S. aureus SH1000 at a probe concentration of 100 µM. The data are presented as letter plots, in which the size of each letter is scaled by the fraction of all modified sites that were modified at the indicated amino acid. All amino acids that were modified in fewer than 5% of cases are summarized as ‘Others’. The total numbers of modified sites are given as a bar graph on top of the letter plot. aNo clear mass of modification was detected, and therefore no analysis of the amino acid selectivity was possible. bData for the indicated probe at 1 mM are shown. All data are based on technical duplicates.
