Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing

Citations Over TimeTop 1% of 1994 papers

Abstract

Characterization and verification of the structures of large biomolecules with high-resolution tandem Fourier transform mass spectrometry with electrospray ionization is critically dependent on the technique used to fragment the multiply charged ions produced. Infrared multiphoton dissociation (IRMPD) of ionized proteins as large as carbonic anhydrase (29 kDa) yields fragment information similar to, but with valuable additions to, that of other dissociation techniques. IRMPD yields product ions on-axis, providing efficient dissociation in further stages; MS3 of ubiquitin (8.6 kDa) yields 11 new sequence ions. Optimum irradiation times for protein ion dissociation vary by more than a factor of 6, with times for oligonucleotides far lower, possibly due to photon resonance with a P-O stretching frequency. IRMPD provides far greater selectivity than collisionally activated dissociation and also appears to yield much less mass discrimination and to dissociate much more stable ions. A technique to remove product ions on formation from the laser beam should improve the present efficiencies of 30-80%.

Related Papers

• → Combined infrared multiphoton dissociation and electron capture dissociation with a hollow electron beam in Fourier transform ion cyclotron resonance mass spectrometry(2003)139 cited
• → 2D FT-ICR MS of Calmodulin: A Top-Down and Bottom-Up Approach(2016)39 cited
• → Combined infrared multiphoton dissociation and electron‐capture dissociation using co‐linear and overlapping beams in Fourier transform ion cyclotron resonance mass spectrometry(2006)27 cited
• → Peptide and protein characterization by high‐rate electron capture dissociation Fourier transform ion cyclotron resonance mass spectrometry(2004)41 cited
• Advanced applications of high performance Fourier transform ion cyclotron resonance mass spectrometry(2014)