Principles of Fourier transform ion cyclotron resonance mass spectrometry and its application in structural biology.
Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry has become increasingly significant within recent years. The inherently ultra-high resolution and mass accuracy allow unequivocal assignments of chemical formulae to be made and further structural elucidation can be conducted through the utilization of tandem mass spectrometry techniques. With the advent of electrospray ionization (ESI), FT-ICR mass spectrometry has become a powerful tool for the investigation of biological macromolecules, such as the study of non-covalent interactions of proteins. In this article, the basic principles are highlighted, some of the techniques employed are described and examples of applications are provided, with particular respect being paid to the field of characterization of biomolecules.
Barrow
Mark P
MP
Institute of Mass Spectrometry and Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK. M.P.Barrow@warwick.ac.uk
Burkitt
William I
WI
Derrick
Peter J
PJ
D000818:Animals; D017357:Cyclotrons; D005583:Fourier Analysis; D007477:Ions; D013058:Mass Spectrometry / Q000379:methods; D025941:Protein Interaction Mapping; D040901:Proteomics; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods
D007477:Ions