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Updated: Aug 4, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
Published on: July 31, 2010
A mass spectrometry method for mapping the interface topography of interacting proteins, illustrated by the
R F Steiner1, S Albaugh, C Fenselau
1Department of Chemistry and Biochemistry, University of Maryland (Baltimore County) 21228.
Abstract:
The shielding of lysine groups from acetylation by acetic anhydride has been used to identify the regions of calmodulin in contact with melittin in the 1:1 complex. The estimation of the degree of acetylation was done by examining cyanogen bromide and cyanogen bromide/trypsin digests by mass spectrometry. Evidence was obtained that lysines-21, -75, and -148 are protected to some extent, with the implication that both the N- and C-terminal lobes and the connecting strand are involved in the interaction.
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