Cold Spring Harbor Laboratory  
Contact Us | Faculty & Staff Directory
Darryl Pappin

Associate Professor
Ph.D., University of Leeds,1984


Contact
pappin@cshl.edu
(516) 367-6882 (p)
 
Our genome can encode hundreds of thousands of different proteins, the molecular machines that do the work that is the basis of life.  I use proteomics, a combination of protein chemistry, mass spectrometry and informatics, to identify precisely which proteins are present in cells - cells from different tissues, developmental stages, and disease states.

Darryl Pappin’s lab develops chemical and computational methods for analysis of proteins and peptides. These are fundamental tools for proteomics, and they are vital in many fields of biological investigation. Proteins and peptides are typically analyzed via mass spectrometry, a method that involves fragmenting samples by colliding them with gas atoms in a vacuum. Masses of the resulting fragments are measured, and computer algorithms match the results with known or predicted molecules whose amino acid sequences are either known or inferred. Pappin has developed search engines for mass spectrometry data that enable investigators to sift hundreds of thousands of experimental spectra at a time for database matches. He also seeks to reduce sample complexity via an approach he calls chemical sorting. This includes the use of chelation to enrich phosphopeptides from the total peptide pool and the use of specific affinity-tagged small-molecule inhibitors to segregate classes of kinases or phosphatases for more specific mass spectroscopic analysis.

Please visit the proteomics shared resource home page.
Scuoppo, C., Miething, C., Lindqvist, L., Reyes, J., Ruse, C., Appelmann, I., Yoon, S., Krasnitz, A., Teruya-Feldstein, J., Pappin, D., Pelletier, J., and Lowe, S.W. 2012. A tumour suppressor network relying on the polyamine-hypusine axis. Nature 487: 244–248.

Krishnan, N., Fu, C., Pappin, D.J., and Tonks, N.K. 2011. H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci. Signal 4: ra86.

Obad, S., dos Santos, C.O., Petri, A., Heidenblad, M., Broom, O., Ruse, C., Fu, C., Lindow, M., Stenvang, J., Straarup, E.M., Hansen, H.F., Koch, T., Pappin, D., Hannon, G.J., and Kauppinen, S. 2011. Silencing of microRNA families by seed-targeting tiny LNAs. Nat. Genet. 43: 371–378. 



Han, H., Pappin, D.J., Ross, P.L., and McLuckey, S.A. 2008. Electron transfer dissociation of iTRAQ labeled peptide ions. J. Proteome Res. 7: 3643–3648.

Zhang, Y., Wolf-Yadlin, A., Ross, P.L., Pappin, D.J., Rush, J., Lauffenburger, D.A., and White, F.M. 2005. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 4: 1240–1250.

Archived Publications