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. 1991 Jul;196(1):120-5.
doi: 10.1016/0003-2697(91)90127-f.

A mass spectrometry method for mapping the interface topography of interacting proteins, illustrated by the melittin-calmodulin system

R F Steiner  1 , S Albaugh, C Fenselau, C Murphy, M Vestling
Affiliations

A mass spectrometry method for mapping the interface topography of interacting proteins, illustrated by the melittin-calmodulin system

R F Steiner et al. Anal Biochem. 1991 Jul.

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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