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Monitoring conformational changes in protein complexes using chemical cross-linking and Fourier transform ion cyclotron resonance mass spectrometry : the effect of calcium binding on the calmodulin-melittin complex
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Novak, Petr, Havlicek, Vladimir, Derrick, Peter J., Beran, Kyle A., Bashir, Sajid and Giannakopulos, Anastassios E. (2007) Monitoring conformational changes in protein complexes using chemical cross-linking and Fourier transform ion cyclotron resonance mass spectrometry : the effect of calcium binding on the calmodulin-melittin complex. European Journal of Mass Spectrometry, Volume 13 (Number 4). pp. 281-290. doi:10.1255/ejms.882 ISSN 1469-0667.
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Official URL: http://dx.doi.org/10.1255/ejms.882
Abstract
Calmodulin is an EF hand calcium binding protein. Its binding affinities to various protein/peptide targets often depend on the conformational changes induced by the binding of calcium. One such target is melittin, which binds tightly to calmodulin in the presence of calcium, and inhibits its function. Chemical cross-linking combined with Fourier transform ion cyclotron resonance mass spectrometry has been employed to investigate the coordination of calmodulin and melittin in the complex at different concentrations of calcium. This methodology can be used to monitor structural changes in proteins induced by ligand binding and to study the effects these changes have on non-covalent interactions between proteins. Cross-linking results indicate that the binding place of the first melittin in the calcium-free calmodulin form is the same as in the calcium-loaded calmodulin/melittin complex.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QC Physics | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
Journal or Publication Title: | European Journal of Mass Spectrometry | ||||
Publisher: | I M Publications | ||||
ISSN: | 1469-0667 | ||||
Official Date: | 2007 | ||||
Dates: |
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Volume: | Volume 13 | ||||
Number: | Number 4 | ||||
Number of Pages: | 10 | ||||
Page Range: | pp. 281-290 | ||||
DOI: | 10.1255/ejms.882 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published |
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