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. Author manuscript; available in PMC: 2015 Mar 20.
Published in final edited form as: Nat Protoc. 2014 May 8;9(6):1301–1319. doi: 10.1038/nprot.2014.075

Figure 5. CDSiL-MS based monitoring of conformational rearrangements at critical structural elements of the β2AR.

Figure 5

(a) Cytoplasmic view of β2AR (PDB: 2RH1), showing relative positions of C327 at TM7 (yellow sphere), and K263 (blue sphere) at TM6. (b) Singly charged ion ([M+H]+) isotope-peak pair corresponding to a chymotryptic peptide (327CRSPDFRIAF336) modified at C327 by a light and heavy NEM (m/z 1336.6 and 1341.7, respectively; Δm/z = 5). (c) Singly charged ion ([M+H]+) isotope-peak pair corresponding to a chymotryptic peptide (259RRSSKF264) modified at K263 by light and heavy succinic anhydride (m/z 880.5 and 884.5, respectively; Δm/z = 4).