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Dr David TF Dryden
e-mail: david.dryden@ed.ac.uk tel: 0131 650 4735

Research Interests: protein-DNA interactions, bio-molecular machines, protein mimics of DNA structure, fluorescence spectroscopy, single-molecule imaging, prokaryotic DNA restriction and modification systems

I am interested in all aspects of protein and DNA structure and dynamics with particular emphasis on combining physical and biological techniques at the "interface" between the physical and life sciences. Current research projects are:

  1. Smart biomolecular machines- the type I DNA restriction enzymes
  2. DNA mimicry by proteins for the control of gene transfer
  3. Nucleotide base flipping and DNA distortion- fluorescence of 2-aminopurine
  4. Fluorescence lifetime imaging and microfluidics for protein folding and Enzymology
Smart molecular machines - DNA cleavageDNA mimicry by proteins Nucleotide base flipping

SELECTED RECENT PUBLICATIONS

  1. High-information-content FRET measurements in fixed and living cells using widefield photon-counting FLIM. M. Millington et al. Biophysical Chemistry. [2007] in press.
  2. DNA Mimicry by Proteins and the control of enzymatic activity on DNA. D.T.F. Dryden. Trends in Biotechnology. [2006] 24, 378-382.
  3. Strong physical constraints on sequence-specific target location by proteins on DNA molecules. H. Flyvbjerg et al. Nucleic Acids Res. [2006] 34, 2550–2557.
  4. A Definitive Fluorescence Signature of DNA Base Flipping. R.K. Neely et al. Nucleic Acids Res., [2006] 33, 7138-7150.
  5. The Biology of Restriction and Anti-restriction. M.R. Tock and D.T.F. Dryden. Current Opinion in Microbiology. 8, 466-472 [2005].
  6. DNA bending by M.EcoKI methyltransferase drives nucleotide flipping. T.J. Su et al. Nucleic Acids Res. [2005]; 33, 3235 – 3244.
  7. Reeling in the bases. D.T.F. Dryden. Nature Structural and Molecular Biology. [2004] 11, 804 – 806.
  8. Single molecule fluorescent imaging and its application to the study of DNA condensation. T.J. Su et al. J. Fluorescence [2003] 14, 65-69.
  9. Structure of Ocr from Bacteriophage T7, a Protein that Mimics B-Form DNA. M.D. Walkinshaw et al.. Molecular Cell [2002] 9, 187–194
  10. Direct observation of DNA translocation and cleavage by the EcoKI endonuclease using atomic force microscopy. D. Ellis et al. [1999] Nature Struct. Biol. 6, 15-17.
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