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Träfflista för sökning "WFRF:(Jones J. I) srt2:(1990-1994)"

Sökning: WFRF:(Jones J. I) > (1990-1994)

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  • Jones, R, et al. (författare)
  • Ab initio calculations of the structure and dynamics of C60 and C3- 60
  • 1992
  • Ingår i: Philosophical Magazine Letters. - : Informa UK Limited. - 0950-0839 .- 1362-3036. ; 65:6, s. 291-298
  • Tidskriftsartikel (refereegranskat)abstract
    • A local-density-functional cluster method is used to calculate the structure and vibrational modes of C60. We find C–C lengths in good agreement with observed values. The effect of doping the molecule with three extra electrons is investigated and shown to result in a surprising shortening of the longer bonds. The second derivatives of the energy are evaluated and have enabled, for the first time, all the normal modes of the molecule to be found. We find these to be in fair agreement with the available experimental results.
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  • Sinning, I, et al. (författare)
  • Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
  • 1993
  • Ingår i: J Mol Biol. - 0022-2836. ; 232:1, s. 192-212
  • Tidskriftsartikel (refereegranskat)abstract
    • The crystal structure of human alpha class glutathione transferase A1-1 has been determined and refined to a resolution of 2.6 A. There are two copies of the dimeric enzyme in the asymmetric unit. Each monomer is built from two domains. A bound inhibitor, S-benzyl-glutathione, is primarily associated with one of these domains via a network of hydrogen bonds and salt-links. In particular, the sulphur atom of the inhibitor forms a hydrogen bond to the hydroxyl group of Tyr9 and the guanido group of Arg15. The benzyl group of the inhibitor is completely buried in a hydrophobic pocket. The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain". The main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site.
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