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. Author manuscript; available in PMC: 2017 Apr 14.
Published in final edited form as: J Proteomics. 2016 Feb 18;138:40–47. doi: 10.1016/j.jprot.2016.02.009

Fig. 1. Identification of biotinylated-Cys609 in FESCSVPR of sGC α subunit by LC/MS/MS.

Fig. 1

(a) HCD spectrum of a doubly-charged ion at m/z 676.80. (b) CID spectrum of a doubly-charged ion at m/z 676.81. The biotinylated-Cys site was located on Cys609 in sGC α subunit. Both spectra contain almost complete series of the y+ and b+ ions with the biotinylated-Cys (+428.19 at Cys) found between b3 and b4, as well as between y4 and y5 ions. More y+ ions were observed from the HCD spectrum compared to the CID spectrum, due to the superior capability of HCD to detect low mass fragments.