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  • 1.
    Bergkvist, Anders
    et al.
    Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden / Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, USA.
    Ejdebäck, Mikael
    University of Skövde, Department of Natural Sciences. Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.
    Ubbink, Marcellus
    Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, The Netherlands.
    Karlsson, B. Göran
    Department of Molecular Biotechnology, Chalmers University of Technology, Göteborg, Sweden.
    Surface interactions in the complex between cytochrome f and the E43Q/D44N and E59K/E60Q plastocyanin double mutants as determined by (1)H-NMR chemical shift analysis2001In: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 10, no 12, p. 2623-2626Article in journal (Refereed)
    Abstract [en]

    A combination of site-directed mutagenesis and NMR chemical shift perturbation analysis of backbone and side-chain protons has been used to characterize the transient complex of the photosynthetic redox proteins plastocyanin and cytochrome f. To elucidate the importance of charged residues on complex formation, the complex of cytochrome f and E43Q/D44N or E59K/E60Q spinach plastocyanin double mutants was studied by full analysis of the (1)H chemical shifts by use of two-dimensional homonuclear NMR spectra. Both mutants show a significant overall decrease in chemical shift perturbations compared with wild-type plastocyanin, in agreement with a large decrease in binding affinity. Qualitatively, the E43Q/D44N mutant showed a similar interaction surface as wild-type plastocyanin. The interaction surface in the E59K/E60Q mutant was distinctly different from wild type. It is concluded that all four charged residues contribute to the affinity and that residues E59 and E60 have an additional role in fine tuning the orientation of the proteins in the complex.

  • 2.
    Brodin, Anders
    et al.
    Department of Theoretical Ecology, Lund University, Sweden.
    Jönsson, K. Ingemar
    Department of Theoretical Ecology, Lund University, Sweden.
    Holmgren, Noél
    University of Skövde, Department of Natural Sciences.
    Optimal energy allocation and behaviour in female raptorial birds during the nestling period2003In: Ecoscience, ISSN 1159-6860, Vol. 10, no 2, p. 140-150Article in journal (Refereed)
    Abstract [en]

    In many raptors and owls the male is the main provider of food in the early phase of the nestling period while the female incubates the eggs and broods the young. In the nestling period the female often helps the male to feed the young, but the factors affecting whether and when she leaves the brood to hunt have not been investigated in detail. We present a dynamic state variable model that analyses female behaviour and fat storage dynamics over the nestling period. The results show that in the first half of the nestling period the female faces a conflict between the need to brood the young and the need to hunt to provision them with food. This conflict arises because the energy needs of the young peak early in the nestling period, at a time when they still cannot thermoregulate and therefore need brooding from the female. The most critical period is the second nestling week, when both female and nestling fat reserves will decrease to low levels. Large female fat reserves in the early nestling period provide a solution to this conflict and are essential for successful breeding. Stochasticity in male provisioning is thus not needed to explain why females should be fat when the eggs hatch. Under normal circumstances, the female broods during the first two weeks and leaves the young only if hunting is absolutely necessary. After the second week the energy requirements are relaxed, and whether the female assists the male in hunting or not depends on factors such as male hunting success, environmental stochasticity, and energy requirements of the young. Our model provides a framework for empirical investigations on female behaviour during breeding in raptors, owls, and other birds with marked division of labour.

  • 3.
    Ejdebäck, Mikael
    et al.
    University of Skövde, Department of Natural Sciences. Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.
    Bergkvist, Anders
    Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.
    Karlsson, B. Göran
    Deptartment of Molecular Biotechnology, Chalmers University of Technology, Göteborg, Sweden.
    Ubbink, Marcellus
    Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, Netherlands.
    Side-chain interactions in the plastocyanin-cytochrome f complex2000In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 39, no 17, p. 5022-5027Article in journal (Refereed)
    Abstract [en]

    Cytochrome f and plastocyanin are redox partners in the photosynthetic electron-transfer chain. Electron transfer from cytochrome f to plastocyanin occurs in a specific short-lived complex. To obtain detailed information about the binding interface in this transient complex, the effects of binding on the backbone and side-chain protons of plastocyanin have been analyzed by mapping NMR chemical-shift changes. Cytochrome f was added to plastocyanin up to 0.3 M equiv, and the plastocyanin proton chemical shifts were measured. Out of approximately 500 proton resonances, 86% could be observed with this method. Nineteen percent demonstrate significant chemical-shift changes and these protons are located in the hydrophobic patch (including the copper ligands) and the acidic patches of plastocyanin, demonstrating that both areas are part of the interface in the complex. This is consistent with the recently determined structure of the complex [Ubbink, M., Ejdebäck, M., Karlsson, B. G., and Bendall, D. S. (1998) Structure 6, 323-335]. The largest chemical-shift changes are found around His87 in the hydrophobic patch, which indicates tight contacts and possibly water exclusion from this part of the protein interface. These results support the idea that electron transfer occurs via His87 to the copper in plastocyanin and suggest that the hydrophobic patch determines the specificity of the binding. The chemical-shift changes in the acidic patches are significant but small, suggesting that the acidic groups are involved in electrostatic interactions but remain solvent exposed. The existence of small differences between the present data and those used for the structure may imply that the redox state of the metals in both proteins slightly affects the structure of the complex. The chemical-shift mapping is performed on unlabeled proteins, making it an efficient way to analyze effects of mutations on the structure of the complex.

  • 4.
    Hare, Kathryn E.
    et al.
    Department of Pure Mathematics, University of Waterloo, Waterloo, Ontario, Canada.
    Rönning, Jan-Olav
    University of Skövde, Department of Natural Sciences.
    Applications of generalized Perron trees to maximal functions and density bases1998In: Journal of Fourier Analysis and Applications, ISSN 1069-5869, E-ISSN 1531-5851, Vol. 4, no 2, p. 215-227Article in journal (Refereed)
  • 5.
    Hare, Kathryn E.
    et al.
    Department of Pure Mathematics, University of Waterloo, Canada.
    Rönning, Jan-Olav
    University of Skövde, Department of Natural Sciences.
    Fractal dimensions of infinite product spaces2004In: International journal of pure and applied mathematics, ISSN 1311-8080, E-ISSN 1314-3395, Vol. 14, no 2, p. 139-167Article in journal (Refereed)
  • 6.
    Hare, Kathryn E.
    et al.
    Department of Pure Mathematics, University of Waterloo, Waterloo, Ontario Canada.
    Rönning, Jan-Olav
    University of Skövde, Department of Natural Sciences.
    The size of Max(p) sets and density bases2002In: Journal of Fourier Analysis and Applications, ISSN 1069-5869, E-ISSN 1531-5851, Vol. 8, no 3, p. 259-268Article in journal (Refereed)
  • 7.
    Jonsson, Malin K. B.
    et al.
    Genome Institute of Singapore, Genome, Singapore.
    van Veen, Toon A. B.
    Department of Medical Physiology, Division of Heart & Lungs, UMC Utrecht, Utrecht, Netherlands.
    Synnergren, Jane
    University of Skövde, Department of Natural Sciences. University of Skövde, School of Bioscience.
    Becker, Bruno
    Department of Psychiatry and Neurochemistry, Sahlgrenska University Hospital, Mölndal, Sweden.
    Towards Creating the Perfect In Vitro Cell Model2016In: Stem Cells International, ISSN 1687-9678, Vol. 2016, article id 3459730Article in journal (Refereed)
  • 8.
    Olesen, Kenneth
    et al.
    Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.
    Ejdebäck, Mikael
    University of Skövde, Department of Natural Sciences. Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.
    Crnogorac, Milan M.
    Department of Chemistry, Iowa State University, Ames, United States.
    Kostić, Nenad M.
    Department of Chemistry, Iowa State University, Ames, United States.
    Hansson, Örjan
    Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.
    Electron transfer to photosystem 1 from spinach plastocyanin mutated in the small acidic patch: ionic strength dependence of kinetics and comparison of mechanistic models1999In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 38, no 50, p. 16695-16705Article in journal (Refereed)
    Abstract [en]

    A set of plastocyanin (Pc) mutants, probing the small acidic patch (Glu59, Glu60, and Asp61) and a nearby residue, Gln88, has been constructed to provide further insight into the electron transfer process between Pc and photosystem 1. The negatively charged residues were changed into their neutral counterparts or to a positive lysine. All mutant proteins exhibited electron transfer kinetics qualitatively similar to those of the wild type protein over a wide range of Pc concentrations. The kinetics were slightly faster for the Gln88Lys mutant, while they were significantly slower for the Glu59Lys mutant. The data were analyzed with two different models: one involving a conformational change of the Pc-photosystem 1 complex that precedes the electron transfer step (assumed to be irreversible) [Bottin, H., and Mathis, P. (1985) Biochemistry 24, 6453-6460] and another where no conformational change occurs, the electron transfer step is reversible, and dissociation of products is explicitly taken into account [Drepper, F., Hippler, M., Nitschke, W., and Haehnel, W. (1996) Biochemistry 35, 1282-1295]. Both models can account for the observed kinetics in the limits of low and high Pc concentrations. To discriminate between the models, the effects of added magnesium ions on the kinetics were investigated. At a high Pc concentration (0.7 mM), the ionic strength dependence was found to be consistent with the model involving a conformational change but not with the model where the electron transfer is reversible. One residue in the small acidic patch, Glu60, seems to be responsible for the major part of the ionic strength dependence of the kinetics.

  • 9.
    Rönning, Jan-Olav
    University of Skövde, Department of Natural Sciences.
    A convergence result for square roots of the Poisson kernel in the bidisk1999In: Mathematica Scandinavica, ISSN 0025-5521, E-ISSN 1903-1807, Vol. 84, no 1, p. 81-92Article in journal (Refereed)
  • 10.
    Rönning, Jan-Olav
    University of Skövde, Department of Natural Sciences.
    Convergence results for the square root of the Poisson kernel1997In: Mathematica Scandinavica, ISSN 0025-5521, E-ISSN 1903-1807, Vol. 81, no 2, p. 219-235Article in journal (Refereed)
  • 11.
    Rönning, Jan-Olav
    et al.
    University of Skövde, Department of Natural Sciences.
    Svensson, Olof
    Linköpings Universitet, Campus Norrköping, Institutionen för teknik och naturvetenskap.
    Convergence for the square root of the Poisson kernel in rank one symmetric spaces against boundary functions with regularity: Preprint Chalmers och Göteborgs Universitet, (79)2001Manuscript (preprint) (Other academic)
1 - 11 of 11
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