Search Results - "Kadima, W."

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  1. 1

    Characterization of precrystallization aggregation of canavalin by dynamic light scattering by Kadima, W., McPherson, A., Dunn, M.F., Jurnak, F.A.

    Published in Biophysical journal (1990)
    “…The aggregation processes leading to crystallization and precipitation of canavalin have been investigated by dynamic light scattering (DLS) in photon…”
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    Journal Article
  2. 2

    The influence of ionic strength and pH on the aggregation properties of zinc-free insulin studied by static and dynamic laser light scattering by Kadima, W, Ogendal, L, Bauer, R, Kaarsholm, N, Brodersen, K, Hansen, J F, Porting, P

    Published in Biopolymers (01-11-1993)
    “…The aggregation properties of zinc-free insulin have been studied using static and dynamic light scattering. The aggregation has been investigated as a…”
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  3. 3

    Role of Metal Ions in the T- To R-Allosteric Transition in the Insulin Hexamer by Kadima, Webe

    Published in Biochemistry (Easton) (12-10-1999)
    “…The role of metal ions in the T- to R-allosteric transition is ascertained from the investigation of the T- to R-allosteric transition of transition metal ions…”
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  4. 4

    Studies of the association and conformational properties of metal-free insulin in alkaline sodium chloride solutions by one- and two-dimensional 1H NMR by KADIMA, W, ROY, M, LEE, R. W.-K, KAARSHOLM, N. C, DUNN, M. F

    Published in The Journal of biological chemistry (05-05-1992)
    “…One- and two-dimensional 1H NMR spectroscopy have been employed to probe the association and subsequent conformational changes of metal-free insulin in sodium…”
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  5. 5

    Structural signatures of the complex formed between 3‐nitro‐4‐hydroxybenzoate and the Zn(II)‐substituted R 6 insulin hexamer by Olsen, Helle Birk, Leuenberger‐Fisher, Melissa R., Kadima, Webe, Borchardt, Dan, Kaarsholm, Niels C., Dunn, Michael F.

    Published in Protein science (01-09-2003)
    “…3‐Nitro‐4‐hydroxybenzoate (3N4H) is a probe of the structure and dynamics of the metal‐centered His B10 assembly sites of the insulin hexamer. Each His B10…”
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  6. 6

    Nuclear magnetic resonance studies of the solution chemistry of metal complexes. 26. Mixed ligand complexes of cadmium, nitrilotriacetic acid, glutathione, and related ligands by Kadima, W, Rabenstein, D L

    Published in Journal of inorganic biochemistry (01-04-1990)
    “…The complexation of glutathione and related ligands by the nitrilotriacetic acid complex of Cd2+ (Cd(NTA)-) has been investigated by 1H NMR as a model for the…”
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  7. 7

    Studies of the association and conformational properties of metal-free insulin in alkaline sodium chloride solutions by one- and two-dimensional super(1)H NMR by Kadima, W, Roy, M, Lee, RW-K, Kaarsholm, N C, Dunn, M F

    Published in The Journal of biological chemistry (01-01-1992)
    “…One- and two-dimensional super(1)H NMR spectroscopy have been employed to probe the association and subsequent conformational changes of metal-free insulin in…”
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  8. 8

    L-Serine analogs form Schiff base and quinonoidal intermediates with Escherichia coli tryptophan synthase by Houben, Karl F, Kadima, Webe, Roy, Melinda, Dunn, Michael F

    Published in Biochemistry (Easton) (16-05-1989)
    “…Substrate analogues of L-serine have been found that react with the alpha 2 beta 2 complex of Escherichia coli tryptophan synthase. Upon reaction with alpha 2…”
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  9. 9

    A quantitative study of the complexation of cadmium in hemolyzed human erythrocytes by 1H NMR spectroscopy by Kadima, W, Rabenstein, D L

    Published in Journal of inorganic biochemistry (01-10-1990)
    “…The stability of complexes formed by Cd2+ in hemolyzed human erythrocytes was studied by spin-echo 1H NMR spectroscopy. Changes in resonances for the…”
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  10. 10

    A proton nuclear magnetic resonance study of the interaction of cadmium with human erythrocytes by Rabenstein, D L, Isab, A A, Kadima, W, Mohanakrishnan, P

    Published in Biochimica et biophysica acta (14-07-1983)
    “…The binding of Cd2+ by molecules in the intracellular region of human erythrocytes has been studied by 1H-NMR spectroscopy. From changes in spin-echo Fourier…”
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