Craggs Timothy D.

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Timothy D. Craggs


Dr Tim Craggs obtained his MSci in Chemistry from the University of Cambridge in 2002. After his PhD (Cambridge 2007) and a postdoc in St Andrews, he took up a Lindemann Fellowship at Yale University (2010), followed by senior postdoc positions at Oxford (Kapanidis Lab) and Bristol (Dillingham Lab). In 2016 he was appointed to a Lectureship in Chemical Biology at the University of Sheffield.

Research Interests Single-molecule approaches provide unprecedented detail to the understanding of essential biological processes, as was recognized in the awarding of the 2014 Nobel Prize for Chemistry. Their unique advantage stems from the ability to go beyond the ensemble- and time-averaging of common biochemical techniques, enabling the identification and interpretation of asynchronous reactions, transient states, and rare sub-species.

Research in the Craggs Lab involves the development and application of single-molecule fluorescence techniques to addressing crucial questions across physics, chemistry and the life sciences.

Recent work has focussed on the development and application of single-molecule fluorescence resonance energy transfer (smFRET – a molecular ruler for the 30-90 Å scale) to questions of protein folding, and DNA transcription, replication and repair. These methods are capable of observing individual molecules and molecular interactions in real time, and understanding their dynamics.

In addition to this mechanistic work, we have shown we can use smFRET to measure absolute distances with angstrom accuracy, opening the door to FRET driven structural biology.

Selected Publications

  • Craggs TD (2017) Cool and dynamic: single-molecule fluorescence-based structural biology. Nature Methods, 14(2), 123-124.
  • Nott TJ, Craggs TD & Baldwin AJ (2016) Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters. Nature Chemistry, 8(6), 569-575.
  • Meli M, Sustarsic M, Craggs TD, Kapanidis AN & Colombo G (2016) DNA Polymerase Conformational Dynamics and the Role of Fidelity-Conferring Residues: Insights from Computational Simulations. Frontiers in Molecular Biosciences, 3. View this article in WRRO
  • Algasaier SI, Exell JC, Bennet IA, Thompson MJ, Gotham VJB, Shaw SJ, Craggs TD, Finger LD & Grasby JA (2016) DNA and Protein Requirements for Substrate Conformational Changes Necessary for Human Flap Endonuclease-1-catalyzed Reaction. Journal of Biological Chemistry, 291(15), 8258-8268. View this article in WRRO
  • Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs TD, Bazett-Jones DP, Pawson T, Forman-Kay JD & Baldwin AJ (2015) Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles. Molecular Cell, 57(5), 936-947.
  • Blouin S, Craggs TD, Lafontaine DA & Penedo JC (2015) Functional studies of DNA-protein interactions using FRET techniques, 1334, 115-141.
  • Hohlbein J, Craggs TD & Cordes T (2014) Alternating-laser excitation: single-molecule FRET and beyond. Chem. Soc. Rev., 43(4), 1156-1171.
  • Craggs TD, Hutton RD, Brenlla A, White MF & Penedo JC (2014) Single-molecule characterization of Fen1 and Fen1/PCNA complexes acting on flap substrates. Nucleic Acids Research, 42(3), 1857-1872.
  • Hohlbein J, Craggs TD & Cordes T (2014) Alternating-laser excitation: single-molecule FRET and beyond (vol 43, pg 1156, 2014). CHEMICAL SOCIETY REVIEWS, 43(17), 6472-6472. (2014) Additions and corrections published 30th October 2013 to 15th July 2014. Chemical Society Reviews, 43(17), 6470-6470.
  • Hohlbein J, Aigrain L, Craggs TD, Bermek O, Potapova O, Shoolizadeh P, Grindley NDF, Joyce CM & Kapanidis AN (2013) Conformational landscapes of DNA polymerase I and mutator derivatives establish fidelity checkpoints for nucleotide insertion. Nature Communications, 4.
  • Robb NC, Cordes T, Hwang LC, Gryte K, Duchi D, Craggs TD, Santoso Y, Weiss S, Ebright RH & Kapanidis AN (2013) The Transcription Bubble of the RNA Polymerase–Promoter Open Complex Exhibits Conformational Heterogeneity and Millisecond-Scale Dynamics: Implications for Transcription Start-Site Selection. Journal of Molecular Biology, 425(5), 875-885.
  • Craggs TD & Kapanidis AN (2012) Six steps closer to FRET-driven structural biology. Nature Methods, 9(12), 1157-1158.
  • Hutton RD, Craggs TD, White MF & Penedo JC (2010) PCNA and XPF cooperate to distort DNA substrates. Nucleic Acids Research, 38(5), 1664-1675.
  • Craggs TD (2009) Green fluorescent protein: structure, folding and chromophore maturation. Chemical Society Reviews, 38(10), 2865-2865.
  • Blouin S, Craggs TD, Lafontaine DA & Penedo JC (2009) Functional studies of DNA-protein interactions using FRET techniques. Methods in Molecular Biology, 543, 475-502.
  • Orte A, Craggs TD, White SS, Jackson SE & Klenerman D (2008) Evidence of an Intermediate and Parallel Pathways in Protein Unfolding from Single-Molecule Fluorescence. Journal of the American Chemical Society, 130(25), 7898-7907.
  • Huang J-R, Craggs TD, Christodoulou J & Jackson SE (2007) Stable Intermediate States and High Energy Barriers in the Unfolding of GFP. Journal of Molecular Biology, 370(2), 356-371.
  • Kuprov I, Craggs TD, Jackson SE & Hore PJ (2007) Spin Relaxation Effects in Photochemically Induced Dynamic Nuclear Polarization Spectroscopy of Nuclei with Strongly Anisotropic Hyperfine Couplings. Journal of the American Chemical Society, 129(29), 9004-9013.
  • Khan F, Kuprov I, Craggs TD, Hore PJ & Jackson SE (2006) 19 F NMR Studies of the Native and Denatured States of Green Fluorescent Protein. Journal of the American Chemical Society, 128(33), 10729-10737.
  • Jackson SE, Craggs TD & Huang J-R (2006) Understanding the folding of GFP using biophysical techniques. Expert Review of Proteomics, 3(5), 545-559.