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

✍ Scribed by Robert F. Steiner; Sharon Albaugh; Catherine Fenselau; Constance Murphy; Martha Vestling


Publisher
Elsevier Science
Year
1991
Tongue
English
Weight
679 KB
Volume
196
Category
Article
ISSN
0003-2697

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✦ Synopsis


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.