Gavin E Reid

Professor of Bioanalytical Chemistry
School of Chemistry

Department of Biochemistry and Molecular Biology

The University of Melbourne

Bio21 Molecular Science and Biotechnology Institute

30 Flemington Rd, room 470

Parkville Victoria 3010, Australia

Phone(Office): +61 3 8344 2650 

Phone(Mobile): +61 466 554 258 

Email: gavin.reid@unimelb.edu.au

 

 

 


Post Doctoral Research Associate (August 2000-March 2002)

Application of Ion/Ion Reactions for "Top Down" Protein Identification and Characterization in a Quadrupole Ion Trap Mass Spectrometer.

 

Specific Areas of Research:

(i)                 Examination of the charge state dependent fragmentation behavior of multiply charged protein ions.

(ii)                Development of the "ion parking" technique for concentration and purification of multiply charged precursor ions.

(iii)              Application of ion parking to the gas-phase concentration, purification and identification of proteins from complex mixtures of E.coli.

(iv)              Design, modification and evaluation of a new quadrupole ion trap mass spectrometer adapted for ion-ion reaction studies.

 

Publications arising from Post Doctoral Research:

Reid, G.E. Wells, J.M., Badman, E.R. and McLuckey S.A. (2002) Performance of a quadrupole ion trap mass spectrometer adapted for ion-ion reaction studies. Int. J. Mass Spectrom. In Press. 

He, M, Reid, G.E. Shang, H-S., Lee, G.U. and McLuckey, S.A. (2002) Product ion formation from multiple parent ion charge states following gas-phase protein ion purification and concentration. Anal. Chem. In Press.

Engel, B.J. Pan, P. Reid, G.E., Wells, J.M. and McLuckey, S.A. (2002) Charge state dependent fragmentation of gaseous protein ions in a quadrupole ion trap: Bovine ferri-, ferro-, and apo-cytochrome c. Int. J. Mass Spectrom. In Press.

Reid, G.E. and McLuckey, S.A. (2002) "Top down" protein identification and characterization via tandem mass spectrometry. In: 'Proteomics: A Laboratory Manual' by Simpson, R.J. Cold Spring Harbor Laboratory Press. In Press.

Reid, G.E. and McLuckey, S.A. (2002) "Top down" protein characterization via tandem mass spectrometry. J. Mass Spectrom. 37: 663-675.

Reid, G.E., Shang, H., Hogan, J., Lee, G.U. and McLuckey S.A. (2002) Gas-phase concentration, purification and identification of whole proteins from complex mixtures. J. Am. Chem. Soc. 124: 7353-7362.

Stephenson, J.L., McLuckey, S.A., Reid, G.E., Wells, J.M. and Bundy, J.L. (2002) The detection and identification of intact proteins from complex mixtures using ion/ion chemistry: Current status and future implications. Curr. Opin. Biotechnol. 13: 57-64.

Reid, G.E. and McLuckey, S.A. (2002) Tandem mass spectrometry of ribonuclease A and B: N-linked glycosylation site analysis of whole protein ions. Anal. Chem. 74: 577-583.

McLuckey, S.A. Reid, G.E. Wells, J.M. (2002) Ion parking during ion/ion reactions in electrodynamic ion traps. Anal. Chem. 74: 336-346. 

Newton, K.A., Chrisman, P.A., Reid, G.E., Wells, J.M. and McLuckey, S.A. (2001) Gaseous apomyoglobin ion dissociation in a quadrupole ion trap: [M+4H]4+ - [M+21H]21+. Int. J. -.Mass Spectrom. 212: 359-376. 

Chrisman, P.A., Newton, K.A., Reid, G.E., Wells, J.M. and McLuckey, S.A. (2001) Loss of charged versus neutral heme from gaseous holomyoglobin ions. Rapid. Commun. Mass Spectrom. 15: 2334-2340. 

Wells, J.M., Reid, G.E., Engel, B.J., Pan, P. and McLuckey, S.A. (2001) Dissociation reactions of gaseous ferro-, ferri-, and apo-cytochrome c ions. J. Am. Soc. Mass Spectrom. 12: 873-876. 

Reid, G.E., Wu, J., Chrisman, P.A., Wells, J.M. and McLuckey, S.A. (2001) Charge state dependance on the sequence analysis of protonated ubiquitin ions by tandem mass spectrometry and ion/ion reactions. Anal. Chem. 73: 3274-3281.

 

Current Research Interests: Bioanalytical Mass Spectrometry and Proteomics. 

My research focuses on the development and application of novel chemical and mass spectrometry based approaches for the identification, structural characterization and quantitation of proteins present in complex biological mixtures, with particular emphasis on characterization of the proteins and protein complexes involved in signalling pathways associated with cancer development.