Gavin E. Reid

Research Interests

The mixture complexity, dynamic range and diversity of transcriptional, translation and post translational modifications associated with protein expression, as well as the complex array of specific protein-protein interactions involved in the regulation of cellular function, presents a significant analytical challenge to mass spectrometry (MS) based proteomic methods employed for characterization of the hitherto unknown functional role of the thousands of genes identified from recent genome sequencing initiatives.

Research in our laboratory is broadly directed toward the development and application of novel mass spectrometry based chemistries and instrumentation to address these challenges. Aspects of this research include:
(i) systematic examination of the fundamental gas-phase ion chemistries of amino acids, peptides and proteins in order to determine the mechanisms and other factors influencing their fragmentation reactions;

The presence of post-translationally modified (PTM) amino acid residues within a peptide sequence often has a dramatic effect on the fragmentation behavior of its protonated ions under low energy collision induced dissociation (CID) tandem mass spectrometry (MS/MS) conditions. MORE

Recent Publications

Griffitts, J., Tesiram, Y., Reid, G.E., Saunders, D., Floyd, R. and Towner, R. (2009) In Vivo magnetic resonance spectroscopy (MRS) assessment of altered fatty acyl unsaturation in liver tumor formation of a TGFα/c-myc transgenic mouse model. J. Lipid. Res. In Press.

Dunn, J.D., Reid, G.E. and Bruening, M.L. (2009) Enrichment of Phosphopeptides Prior to Analysis by Mass Spectrometry. Mass Spectrom. Rev. In Press.

Froelich, J.M., Lu, Y. and Reid, G.E. (2009) Chemical Derivatization and Multistage Tandem Mass Spectrometry for Protein Structural Characterization. In: Practical Aspects of Trapped Ion Mass Spectrometry. Vol. 5: Applications. (R.E. March and J.F.J. Todd. Ed), CRC Press. In Press.

Zhang, X., Ferguson-Miller, S.M. and Reid, G.E. (2009) Characterization of Ornithine and Glutamine Lipids Extracted from Cell Membranes of Rhodobacter sphaeroides. J. Am. Soc. Mass Spectrom. 20(2):198-212.

Froelich, J.M. and Reid, G.E. (2009) The Effect of Post-translational and Process-induced Modifications on the Multistage Gas-Phase Fragmentation Reactions of Protonated Peptide Ions. Combinatorial Chemistry and High Throughput Screening. 12(2):175-84.

Palumbo, A.M and Reid, G.E. (2008) Evaluation of Gas-Phase Rearrangement and Competing Fragmentation Reactions on Protein Phosphorylation Site Assignment using CID-MS/MS and MS3. Anal. Chem. 80: 9735-9747.

Lu, Y., Tanasova, M., Borhan, B. and Reid, G.E. (2008) An Ionic Reagent for Controlling the Gas-Phase Fragmentation Reactions of Cross-Linked Peptides. Anal. Chem. 80: 9279-9287.

Froelich, J.M., Kaplinghat, S. and Reid, G.E. (2008) Automated Neutral Loss and Data Dependent Energy Resolved "Pseudo MS3" for the Targeted Identification, Characterization and Quantitative Analysis of Methionine-Containing Peptides. Eur. J. Mass Spectrom. 14: 219-229.

Dunn, J.D., Igrisan, E.A., Palumbo, A.M., Reid, G.E. and Bruening, M.L. (2008) Phosphopeptide Enrichment Using MALDI Plates Modified with High-capacity Polymer Brushes. Anal. Chem. 80: 5727-5735.

Hohmann, L.J., Eng, J.K., Gemmill, A., Klimek, J., Vitek, O., Reid, G.E. and Martin D. B. (2008) Quantification of the Compositional Information Provided by Immonium Ions on a Quadrupole-TOF Mass Spectrometer. Anal. Chem. 80: 5596-5606.

Froelich, J.M. and Reid, G.E. (2008). The Origin and Control of Ex Vivo Oxidative Peptide Modifications Prior to Mass Spectrometry Analysis. Proteomics. 8: 1334-1345.

Palumbo, A.M., Tepe, J.J. and Reid, G.E. (2008) Mechanistic Insights into the Multistage Gas-Phase Fragmentation Behavior of Phosphoserine- and Phosphothreonine-containing Peptides. J. Proteome Res. 7: 771-779.

Meyer, J., Froelich, J.M., Reid, G.E., Karunarathne, W. and Spence, D. (2008) Metal-activated C-peptide Facilitates Glucose Clearance and the Release of a Nitric Oxide Stimulus via the GLUT1 Transporter. Diabetologia. 51: 175-182.