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. 2019 Apr 26;91(10):6577–6584. doi: 10.1021/acs.analchem.9b00244

Figure 5.

Figure 5

Correlating IV-FPOP modification to solvent accessibility. (a) Myosin chaperon protein UNC-45 (gray) (PDB ID 4I2Z(46)) highlighting two modified peptides identified by LC/MS/MS analysis, 669–680 and 698–706 (green, left inset). UNC-45 is bound to the Hsp90 peptide fragment (blue). Oxidatively modified residues within this fragment are shown in sticks (red), and UNC-45 is rendered as a surface (right inset). (b]) Tandem MS spectra of UNC-45 peptide 669–680 (top) and 698–706 (bottom) showing b- and y-ions for the loss of CO2, an FPOP modification. (c) The calculated ln(PF) for the Hsp90 oxidatively modified residues, R697, M698, E699, and E700. (d) Tandem MS spectra for R697, M698, E699, and E700 showing a +16 FPOP modification.