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• W2029607844 abstract "Chemical cross-linking--an established technique in protein chemistry--has re-emerged, in combination with mass spectrometric analysis of the reaction products, as a valuable tool to identify interacting amino acid sequences in protein complexes. In the present study, we are mapping the interface of the calcium-dependent complex between calmodulin (CaM) and a peptide derived from the C-terminal region of adenylyl cyclase 8 (AC 8). Cross-linking reactions are performed using the two amine-reactive, isotope-labeled (d0 and d4) cross-linkers BS(3) (bis[sulfosuccinimidyl]suberate) and BS(2)G (bi[sulfosuccinimidyl] glutarate) as well as the 'zero-length' cross-linker (EDC, ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride). After separation of the cross-linking reaction mixtures by one-dimensional gel electrophoresis (sodium dodecyl sulphate polyacrylamide gel) and in-gel digestion of the cross-linked complexes, the resulting peptide mixtures are analyzed by nano-high-performance liquid chromatography/ nano-electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. The identified intermolecular cross-linking products will give further insight into calmodulin/adenylyl cyclase 8 interaction." @default.
• W2029607844 created "2016-06-24" @default.
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• W2029607844 date "2005-10-01" @default.
• W2029607844 modified "2023-09-30" @default.
• W2029607844 title "Mapping Protein Interfaces by Chemical Cross-Linking and Fourier Transform Ion Cyclotron Resonance Mass Spectrometry: Application to a Calmodulin/Adenylyl Cyclase 8 Peptide Complex" @default.
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• W2029607844 doi "https://doi.org/10.1255/ejms.748" @default.
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