个人简介

B.S. University of Massachusetts, 1962 Ph.D. University of Massachusetts, 1967 NIH Postdoctoral Trainee, Massachusetts Institute of Technology, 1967

研究领域

Analytical biochemistry/mass spectrometry/proteomics

The goal of our research is to develop new methods and instrumentation for the structural characterization of proteins and their post translational modifications at the low femtomole/attomole level and to apply these new methods to important structural problems in cell biology and immunology. Towards this end, we have pioneered the use of nanoflow HPLC in conjunction with microelectrospray ionization on ion trap and Fourier transform mass spectrometers. Briefly stated, the approach involves the use of proteolytic enzymes to convert the protein or group of proteins into a complex mixture of peptides, which are then fractionated by nanoflow-HPLC and eluted directly into the mass spectrometer. Mixtures containing thousands of different peptides can be analyzed in this manner. Protonated peptides of a particular mass are selected under computer control of instrument, fragmented on collision with helium atoms and the resulting fragments are then separated and mass analyzed. Dissociation of the peptide ions occurs more or less randomly at each of the amide bonds in the molecules to produce a collection of fragments. The mass difference between two fragments differing by a single amino acid defines the mass and thus the identity of the extra residue in the longer fragment. Peptide sequence analysis is performed routinely at the femtomole and low attomole levels on the ion trap and Fourier transform instruments, respectively. Mass spectra acquired in the above manner can also be used to search databases and to identify known proteins. Currently, this approach is the most sensitive method in the world for protein characterization.

近期论文

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Front-End Electron Transfer Dissociation: A New Ionization Source. Earley L, Anderson LC, Bai DL, Mullen C, Syka JE, English AM, Dunyach JJ, Stafford GC Jr, Shabanowitz J, Hunt DF, Compton PD. Anal Chem. 2013 Aug 19. [Epub ahead of print] Posttranslational modification of CENP-A influences the conformation of centromeric chromatin. Bailey AO, Panchenko T, Sathyan KM, Petkowski JJ, Pai PJ, Bai DL, Russell DH, Macara IG, Shabanowitz J, Hunt DF, Black BE, Foltz DR. Proc Natl Acad Sci U S A. 110:11827-32 (2013). O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection. Pérez Jde J, Udeshi ND, Shabanowitz J, Ciordia S, Juárez S, Scott CL, Olszewski NE, Hunt DF, García JA. Virology. 2442:122-31 (2013). Site-specific phosphorylation of the DNA damage response mediator rad9 by cyclin-dependent kinases regulates activation of checkpoint kinase 1. Abreu CM, Kumar R, Hamilton D, Dawdy AW, Creavin K, Eivers S, Finn K, Balsbaugh JL, O’Connor R, Kiely PA, Shabanowitz J, Hunt DF, Grenon M, Lowndes NF. PLoS Genet. 9:e1003310 (2013). Peptide-binding motifs associated with MHC molecules common in Chinese rhesus macaques are analogous to those of human HLA supertypes and include HLA-B27-like alleles. Mothé BR, Southwood S, Sidney J, English AM, Wriston A, Hoof I, Shabanowitz J, Hunt DF, Sette A. Immunogenetics. 65:371-86 (2013).