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Träfflista för sökning "WFRF:(Jones A. G.) srt2:(1990-1994)"

Sökning: WFRF:(Jones A. G.) > (1990-1994)

  • Resultat 1-8 av 8
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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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  • Bergfors, T, et al. (författare)
  • Crystallization and preliminary X-ray analysis of recombinant bovine cellular retinoic acid-binding protein.
  • 1994
  • Ingår i: Acta Crystallogr D Biol Crystallogr. - 0907-4449. ; 50:Pt 4, s. 370-4
  • Tidskriftsartikel (refereegranskat)abstract
    • Crystals of bovine cellular retinoic acid-binding protein (CRABPI) have been grown from protein expressed in E. coli. Two different crystal forms were obtained. Crystals containing protein with the ligand all-trans retinoic acid belong to space group P4(1) or P4(3), a = b = 41.36, c = 202.71 A and diffract to 2.5 A. Crystals of CRABP with the synthetic retinoid analogue Am80 diffract to 1.9 A with space group P2(1) and cell dimensions a = 37.03, b = 105.93, c = 40.31 A, beta = 110.28 degrees. Considerations in the crystallization of proteins with light-sensitive ligands are discussed.
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  • Kleywegt, G J, et al. (författare)
  • Detection, delineation, measurement and display of cavities in macromolecular structures.
  • 1994
  • Ingår i: Acta Crystallogr D Biol Crystallogr. - 0907-4449. ; 50:Pt 2, s. 178-85
  • Tidskriftsartikel (refereegranskat)abstract
    • A computer program, VOIDOO, is described which can be employed in the study of cavities such as they occur in macromolecular structures (in particular, in proteins). The program can be used to detect unknown cavities or to delineate known cavities, either of which may be connected to the outside of the molecule or molecular assembly under study. Optionally, output files can be requested that contain a description of the shape of the cavity which can be displayed by the crystallographic modelling program O. Additionally, VOIDOO can be used to calculate the volume of a molecule and to create a file containing data pertaining to the surface of the molecule which can also be displayed using O. Examples of the use of VOIDOO are given for P2 myelin protein, cellular retinol-binding protein and cellobiohydrolase II. Finally, operational definitions to discern different types of cavity are introduced and guidelines for assessing the accuracy and improving the comparability of cavity calculations are given.
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7.
  • Kleywegt, G J, et al. (författare)
  • Halloween ... Masks and Bones
  • 1994
  • Ingår i: From First Map to Final Model. - : SERC Daresbury Laboratory, Daresbury, U.K.. ; , s. 59-66
  • Bokkapitel (övrigt vetenskapligt/konstnärligt)
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  • Resultat 1-8 av 8

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