Edinburgh Research Explorer

Prof Adam Waldman

Chair of Neuroradiology

  1. 1987
  2. A strong carboxylate-arginine interaction is important in substrate orientation and recognition in lactate dehydrogenase

    Hart, K. W., Clarke, A. R., Wigley, D. B., Waldman, A. D., Chia, W. N., Barstow, D. A., Atkinson, T., Jones, J. B. & Holbrook, J. J., 21 Aug 1987, In : Biochimica et biophysica acta-Bioenergetics. 914, 3, p. 294-8 5 p.

    Research output: Contribution to journalArticle

  3. The use of site-directed mutagenesis and time-resolved fluorescence spectroscopy to assign the fluorescence contributions of individual tryptophan residues in Bacillus stearothermophilus lactate dehydrogenase

    Waldman, A. D. B., Clarke, A. R., Wigley, D. B., Hart, K. W., Chia, W. N., Barstow, D., Atkinson, T., Munro, I. & Holbrook, J. J., 1 May 1987, In : Biochimica et biophysica acta-Protein structure and molecular enzymology. 913, 1, p. 66-71

    Research output: Contribution to journalArticle

  4. 1986
  5. 13C-NMR and transient kinetic studies on lactate dehydrogenase [Cys(13CN)165]. Direct measurement of a rate-limiting rearrangement in protein structure

    Waldman, A. D., Birdsall, B., Roberts, G. C. & Holbrook, J. J., 7 Mar 1986, In : Biochimica et biophysica acta-Bioenergetics. 870, 1, p. 102-11 10 p.

    Research output: Contribution to journalArticle

  6. 1985
  7. The rates of defined changes in protein structure during the catalytic cycle of lactate dehydrogenase

    Clarke, A. R., Waldman, A. D. B., Hart, K. W. & John Holbrook, J., 1 Jul 1985, In : Biochimica et biophysica acta-Protein structure and molecular enzymology. 829, 3, p. 397-407

    Research output: Contribution to journalArticle

  8. Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilus

    Clarke, A. R., Waldman, A. D., Munro, I. & Holbrook, J. J., 29 Apr 1985, In : Biochimica et biophysica acta-Bioenergetics. 828, 3, p. 375-9 5 p.

    Research output: Contribution to journalArticle

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