J
Johan P. Turkenburg
Researcher at University of York
Publications - 126
Citations - 8279
Johan P. Turkenburg is an academic researcher from University of York. The author has contributed to research in topics: Hydrolase & Glycoside hydrolase. The author has an hindex of 41, co-authored 124 publications receiving 7492 citations. Previous affiliations of Johan P. Turkenburg include New York University & Newcastle University.
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Journal ArticleDOI
Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi
Nicholas McGregor,Johan P. Turkenburg,Kristian B. R. M. Krogh,Jens Erik Nielsen,Marta Artola,Keith A. Stubbs,Herman S. Overkleeft,Gideon J. Davies +7 more
TL;DR: The structure of a fungal α-l-arabinofuranosidase has been determined using sulfur SAD data collected in vacuo using beamline I23 at Diamond Light Source to provide a detailed map of enzyme–substrate interactions that are conserved between bacteria and fungi.
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Structure and function of a glycoside hydrolase family 8 endoxylanase from Teredinibacter turnerae.
Claire. A. Fowler,Glyn R. Hemsworth,Fiona Cuskin,Sam Hart,Johan P. Turkenburg,Harry J. Gilbert,Paul H. Walton,Gideon J. Davies +7 more
TL;DR: The symbionts of marine shipworms provide a rich reservoir of potential carbohydrate-active enzymes and the 1.5 Å resolution three-dimensional structure of a T. turnerae GH8 xylanase is revealed and its potential in biomass degradation is highlighted.
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DNA-drug refinement: A comparison of the programs NUCLSQ, PROLSQ, SHELXL93 and X-PLOR, using the low-temperature d(TGATCA)-nogalamycin structure
Geertrui S. Schuerman,C.K. Smith,Johan P. Turkenburg,A.N. Dettmar,L. Van Meervelt,Madeleine H. Moore +5 more
TL;DR: Although a different number of water molecules is found in each refinement, varying from 62 (X-PLOR) to 86 (NUCLSQ), the first hydration sphere is well conserved in all four models and the helical parameters and backbone conformation including sugar-puckering modes are not influenced by the refinement procedure used.
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Ring-chain interconversion of sulforhodamine-amine conjugates involves an unusually labile CN bond and allows measurement of sulfonamide ionization kinetics
John E. T. Corrie,John F. Eccleston,Michael A. Ferenczi,Madeleine H. Moore,Johan P. Turkenburg,David R. Trentham +5 more
TL;DR: The pH-dependent interconversion between ring and chain forms of sultams/sulfonamides derived from conjugates of sulforhodamines with amines, and the associated sulfonamide ionization, have been studied by a combination of equilibrium and kinetic methods.
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Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa
TL;DR: In this paper, the catalytic module of a 10 pectate lyase, Pel10A from Pseudomonas cellulosa, was obtained using polyethylene glycol 2000 monomethylether as a precipitant.