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. Author manuscript; available in PMC: 2009 Jun 1.
Published in final edited form as: Mol Immunol. 2008 May 5;45(11):3142–3151. doi: 10.1016/j.molimm.2008.03.010

Fig. 6.

Fig. 6

Detailed structural analysis of peptides 1037–1043 (MALDI) and 1027–1044 (ESI). The diverging HDX results for the MALDI-derived peptide 1037–1043 (−10.4%) and the encompassing peptide 1027–1044 (+1.8%) from ESI analysis can be explained by the relocation of TED during C3 activation. While the common peptide stretch 1037–1043 (yellow) is similarly accessible in both C3 and C3b, the N-terminal elongation of the ESI peptide (1027–1036; red) is buried in C3b and gets exposed in C3b. As a consequence, the signal observed in ESI may be the sum of a HDX decrease (as in MALDI) and an HDX increase (for the N-terminus).