| 1. |
- I. Sinning, G.J. Kleywegt, S.W. Cowan, P. Reinemer, H.W. Dirr, R. Huber, G.L. Gilliland, R.N. Armstrong, X. Ji, P.G. Board, B. Olin, B. Mannervik & T.A. Jones
(författare)
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Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes
- 1993
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Ingår i: Journal of Molecular Biology. ; 232, s. 192-212
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Tidskriftsartikel (refereegranskat)
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| 2. |
- Olin, Håkan, et al.
(författare)
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Scanning tunneling microscopy of oxidized titanium surfaces in air
- 1992
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Ingår i: Ultramicroscopy. - 0304-3991 .- 1879-2723. ; 42:Part A, s. 567-571
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Tidskriftsartikel (refereegranskat)abstract
- Using an STM in air, we have studied three different electropolished Ti surfaces. One sample was analyzed without further treatment. The second was thermally oxidized in air at 500-degrees-C. The third was exposed to an argon glow discharge and then oxidized in pure oxygen. The samples were characterized by Auger spectroscopy prior to STM measurements. Electropolished and thermally oxidized samples showed a granular structure, with a low corrugation between 2 and 10 nm. At a larger scale, the glow discharge treated sample showed a high corrugation approximately 100 nm.
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| 3. |
- Sinning, I, et al.
(författare)
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Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
- 1993
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Ingår i: J Mol Biol. - 0022-2836. ; 232:1, s. 192-212
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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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| 4. |
- Hallander, H, et al.
(författare)
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[New pertussis vaccines are tested].
- 1992
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Ingår i: Läkartidningen. - 0023-7205 .- 1652-7518. ; 89:45, s. 3820-2, 3825
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Tidskriftsartikel (refereegranskat)
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