NMR Facility Coordinator


Matthew James Revington
NMR Facility Coordinator
Department of Chemistry and Biochemistry
University of Windsor
Phone: (519)253-3000, Ext 3997
Email: mrevingt@uwindsor.ca

 

Employment

  • 2008-present
    NMR Facility Co-ordinator
    Department of Chemistry and Biochemistry University of Windsor, Windsor, Ontario, Canada
     
  • 2007-2008
    NMR Staff Scientist
    Department of Structural Biology, St Jude Children’s Research Hospital, Memphis, Tennessee, USA
     
  • 2004-2007
    Research Fellow
    Department of Biochemistry, University of Western Ontario, London, Ontario, Canada
    Supervisor: Dr. Gary Shaw
    Project: NMR Protein Structural Determinations as part of the Ontario Centre for Structural Proteomics
     
  • 2001-2004
    Post-Doctoral Fellow
    Biophysics Research Division, University of Michigan Ann Arbor, Michigan, USA
    Supervisor: Dr. Erik Zuiderweg
    Project: NMR studies of the Allosteric Mechanism of Thermus Thermophilus DnaK

Education

  • PhD: Biochemistry, University of Western Ontario
    Thesis: Structural Studies of the b subunit of Escherichia coli ATP synthase
    Supervisors: Dr. Stanley D. Dunn and Dr. Gary S. Shaw
  • MSc: Medical Biophysics, Ontario Cancer Institute, University of Toronto
    Thesis: NMR Studies of the Escherichia coli trp Repressor Complex with Operator DNA
    Supervisor: Dr. Cheryl H. Arrowsmith
  • BSc: Chemistry and Biochemistry, University of Windsor, Windsor, Ontario, Canada

Teaching Experience

  • Advanced NMR Workshop,  Dept Chemistry and Biochemistry, University of Windsor 2011 and 2012, Created, Lectured and Facilitated
  • Introductory NMR Workshop,  Dept Chemistry and Biochemistry, University of Windsor 2010,2011 and 2012, Created, Lectured
  • Teaching Assiatant 3rd year Biochemistry Laboratory, 1996-2000,
    Department of Bicochemistry, University of Westen Ontario

Publications

  1. Crippen, G.M., Rousaki A., Revington M., Zhang Y. and . Zuiderweg E.R.P.
    SAGA: rapid automatic mainchain NMR assignment for large proteins
    J Biomol NMR 2010
     
  2. Bhattacharya, A., Revington, M., and Zuiderweg, E.R.P., Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins,
    J Mag Res, 2009,.
     
  3. Malik, S. Revington, M., Smith, S. and Shaw, G.S.
    Analysis of the structure human apo-S100B at low temperature indicates an unimodal conformational, distribution is adopted by calcium-free S100 proteins
    Proteins: Structure, Function, and Bioinformatics (2008), 73, 28-42.
     
  4. Revington, M., Semesi, A., Yee, A., Arrowsmith, C.H., and Shaw, G.S.
    The solution structure of E. coli ydhA, a periplasmic β-barrel protein
    J. Biomol. NMR (2006), 35, 295-300
    Revington, M., Semesi, A., Yee, A., Shaw, G.S.
     
  5. Solution structure of the{ the} Escherichia coli protein ydhR: a putative mono-oxygenase
    Protein Sci. (2005) 14, 3115-3120
     
  6. Revington, M., Zhang, Y., Yip, G.N.B., Kurochkin, A.V., and Zuiderweg, E.R.P.
    NMR investigations of allosteric processes in a two-domain Thermus Thermophilus DnaK molecular chaperone
    J. Mol. Biol. (2005), 349, 163-183
     
  7. Revington, M., Holder, T.M., and Zuiderweg, E.R.P.
    NMR study of nucleotide-induced changes in the nucleotide-binding domain of Thermus Thermophilus Hsp70 chaperone DnaK: Implications for the allosteric mechanism
    J. Biol. Chem. (2004), 279, 33958-339678.
  8. Revington, M., and Zuiderweg, E.R.P.
    TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone
    J. Biomol. NMR, (2004), 30,113-114
     
  9.  Lee, C.L., Revington, M., Dunn, S.D., and Petersen, N.O.
    The Lateral Diffusion of Selectively Aggregated Peptides in Giant Unilamellar Vesicles,
    Biophys. J. (2003), 85,1338
     
  10. Revington, M., Dunn, S.D., and Shaw, G.S.
    Folding and stability of the b subunit of the F(1) F(0) ATP synthase.
    Protein Sci. (2002), 11, 1227-1238
     
  11. Dunn, S.D., Bi, Y., and Revington, M.
    A Re-examination of the Structural and Functional Consequences of Mutation of Alanine-128 of the b subunit of Escherichia coli ATP Synthase to Aspartic Acid.
    Biochim. Biophys. Acta (2000) 1459, 521-527
     
  12. Dunn, S.D., Revington, M., Cipriano, D.J., and Shilton, B.H.
    The b Subunit of Escherichia coli ATP Synthase.
    J. Bioenerg. Biomem., (2000), 32, 347-355
     
  13. Dunn, S.D., McLachlin, D.T., and Revington, M.
    The Second Stalk of Escherichia coli ATP Synthase.
    Biochim. Biophys. Acta, (2000), 1458, 356-363
     
  14. Revington, M., McLachlin, D.T., Shaw, G.S., and Dunn, S.D.
    The Dimerization Domain of the b Subunit of the Escherichia coli F1F0-ATPase.
    J. Biol. Chem., (1999), 274, 31094-31101
     
  15. Lee, W., Revington, M., Farrow, N.A., Nakamura, A., Utsunomiya-Tate, N., Miyake, Y., Kainosho, M., and Arrowsmith, C.H.
    Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of [ul-13C/15N]-L-tryptophan.
    J. Biomol. NMR., (1995), 5, 367-375
     
  16. Yamazaki, T., Lee, W., Revington, M., Mattiello, D.L., Dahlquist, F.W., Arrowsmith, C.H., and Kay, L.E.
    An HNCA Pulse Scheme for the Backbone Assignment of 15N,13C,2H-Labelled Proteins: Application to a 37-kDa Trp Repressor-DNA Complex
    J. Am. Chem. Soc.,(1994), 116, 6464-6465
     
  17. Lee., W., Revington, M.J., Arrowsmith, C., and Kay, L.E.
    A pulsed field gradient isotope-filtered 3D 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes.
    FEBS Lett., (1994), 350, 87-90
     
  18. Zhang, H., Zhao, D., Revington, M., Lee, W., Jia, X., Arrowsmith, C., and Jardetzky, O.
    The solution structures of the trp repressor-operator DNA complex
    J. Mol. Biol., (1994), 238, 592-614

Book Chapters

  1. Revington, M.J., Lee, W., and Arrowsmith, C.H.
    Heteronuclear Strategies for the Assignment of Larger protein/DNA complexes: Application to the 37 kDa trp Repressor- Operator Complex, Biological NMR Spectroscopy, Edited J. Markley and S. Opella, Oxford Press, (1997), p50-66
     
  2. Arrowsmith, C.H., Lee, W., Revington, M., Yamazaki, T., and Kay, L.E.
    Towards the Solution Structure of Large (>30kDa) Proteins and Macromolecular Complexes, Techniques in Protein Chemistry VI, Academic Press, (1995), p503-547