TAILIEUCHUNG - Báo cáo khoa học: Prion protein library of recombinant constructs for structural biology

A survey of plasmids for 51 prion protein constructs from bank vole, cat, cattle, chicken, dog, elk, ferret, frog, fugu, horse, human, pig, sheep, turtle, and wallaby, and for 113 mouse prion protein constructs and variants thereof, is presented. This includes information on the biochemistry of the recombinant proteins, in particular on successful and unsuccessful expres-sion attempts. | ỊFEBS Journal Prion protein library of recombinant constructs for structural biology Simone Hornemann Ị Barbara ChristenỊ Christine von Schroetter Daniel R. Perez and Kurt Wuthrich Institute of Molecular Biology and Biophysics ETH Zurich Switzerland Keywords NMR structure determination prion protein plasmid library prion protein structural biology recombinant prion proteins transmissible spongiform encephalopathies Correspondence K. Wuthrich Institute of Molecular Biology and Biophysics ETH Zurich CH-8093 Zurich Switzerland Fax 41 44 633 1151 Tel 41 44 633 2473 E-mail wuthrich@ Website http groups wuthrich_group Present address Institute of Neuropathology Universitats- Spital Zurich Switzerland ỊThese authors contributed equally to this work A survey of plasmids for 51 prion protein constructs from bank vole cat cattle chicken dog elk ferret frog fugu horse human pig sheep turtle and wallaby and for 113 mouse prion protein constructs and variants thereof is presented. This includes information on the biochemistry of the recombinant proteins in particular on successful and unsuccessful expression attempts. The plasmid library was generated during the past 12 years in the context of NMR structure determination and biophysical characterization of prion proteins in our laboratory. The plasmids are now available for general use and are distributed free of charge to not-for-profit institutions. Received 23 December 2008 revised 12 February 2009 accepted 13 February 2009 doi Expression of the prion protein PrP in its cellular form PrPC in healthy organisms is intimately related to susceptibility to transmissible spongiform encephalopathies such as scrapie in sheep bovine spongiform encephalopathy chronic wasting disease in deer and Creutzfeldt-Jakob disease in humans 1 . Transmissible spongiform encephalopathies are related to the conversion of PrPC to a protease-resistant b-sheet-rich scrapie form 2 .

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