Jones, Dafydd - Cardiff University - School of Biosciences

个人简介

After gaining my BSc in Biochemistry from the University of Wales, I studied for my PhD in protein structure and engineering at Cambridge University under the supervision of Prof Richard Perham, being awarded my doctorate degree in 1999. My further research has centered on protein structure and engineering, having held research positions in both the academic (MRC Centre for Protein Engineering in Cambridge and the Department of Chemistry, Cambridge University) and industrial (Marie Curie Industrial Fellowship at Novozymes A/S Copenhagen, Denmark) sectors. I moved to Cardiff in September 2003. Amongst my various teaching duties, I am coordinator for the Professional Training Year (sandwich) program for the Biomolecular degree schemes.

研究领域

The main focus of my research group is exploring the structural and functional plasticity of proteins. Our research involves the study and engineering of specific protein systems, construction of artificial protein scaffolds and utilisation of expanded genetic code for non-natural amino acid incorporation. Much of the group's work has a basis in synthetic biology whereby we construct new protein components or modify existing proteins for new applications, including single molecule electron transfer. Both rational protein engineering and directed evolution are used to create new proteins and structural biology, single molecule analysis, molecular dynamics, biophysics and biochemistry are used to investigate the properties of these novel proteins. We have also recently developed several transposon-based methods for the directed evolution of proteins using non-homologous recombination.

近期论文

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Hartley, A.et al. 2016. Molecular basis for functional switching of GFP by two disparate non-native post-translational modifications of a phenyl azide reaction handle. Chemical Science 7(10), pp. 6484-6491. (10.1039/C6SC00944A) Reddington, S.et al. 2015. Genetically encoded phenyl azide photochemistry drives positive and negative functional modulation of a red fluorescent protein. RSC Advances 5(95), pp. 77734-77738. (10.1039/C5RA13552D) pdf Arpino, J.et al. 2015. In-frame amber stop codon replacement mutagenesis for the directed evolution of proteins containing non-canonical amino acids: ientification of residues open to bio-orthogonal modification. PLoS ONE 10(5), article number: e0127504. (10.1371/journal.pone.0127504) pdf Hartley, A.et al. 2015. Functional modulation and directed assembly of an enzyme through designed non-natural post-translation modification. Chemical Science 6(7), pp. 3712-3717. (10.1039/C4SC03900A) pdf Reddington, S.et al. 2015. Directed evolution of GFP with non-natural amino acids identifies residues for augmenting and photoswitching fluorescence. Chemical Science 6(2), pp. 1159-1166. (10.1039/C4SC02827A) pdf Jones, D.et al. 2014. Transposon-based approaches for generating novel molecular diversity during directed evolution. Methods in Molecular Biology 1179, pp. 159-172. (10.1007/978-1-4939-1053-3_11) pdf Arpino, J.et al. 2014. Random single amino acid deletion sampling unveils structural tolerance and the benefits of helical registry shift on GFP folding and structure. Structure 22(6), pp. 889-898. (10.1016/j.str.2014.03.014) pdf Arpino, J. A. J., Rizkallah, P. and Jones, D. D. 2014. Structural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent protein. Acta Crystallographica Section D Biological Crystallography 70(8), pp. 2152-2162. (10.1107/S139900471401267X) pdf