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. Author manuscript; available in PMC: 2012 Nov 4.
Published in final edited form as: J Proteome Res. 2011 Sep 28;10(11):4948–4958. doi: 10.1021/pr200403c

Figure 1.

Figure 1

Schematic representation of the protocol used in this work. A protein mixture is incubated in the presence and absence of ligand before diluting into a series of denaturant-containing buffers. Following SPROX analysis, trypsin digestion, and iTRAQ labeling with the eight different iTRAQ reagents bearing the 113 – 121 reporter ions, the samples across the range of denaturants are combined (i.e., the −ligand samples labeled with the eight iTRAQ reagents bearing the 113–121 reporter ions are combined and the +ligand samples labeled with the eight iTRAQ reagents bearing the 113–121 reporter ions are combined). Ultimately, the − and + ligand samples are each subjected to a Met peptide selection strategy. The samples enriched for Met peptides are analyzed by LC-MS/MS, and iTRAQ reporter ions are used to generate chemical denaturation data.