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  • 1
    Digitale Medien
    Digitale Medien
    The Role of Electrostatic Interactions for Cytochrome c Oxidase Function (1998)
    Springer
    Journal of bioenergetics and biomembranes 30 (1998), S. 81-87 
    Details
    ISSN: 1573-6881
    Schlagwort(e): Protein electrostatics ; Poisson–Boltzmann equation ; proton transfer ; cytochrome c oxidase ; Paracoccus denitrificans
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Physik
    Notizen: Abstract In recent years, the enormous increase in high-resolution three-dimensional structures of proteins together with the development of powerful theoretical techniques have provided the basis for a more detailed examination of the role of electrostatics in determining the midpoint potentials of redox-active metal centers and in influencing the protonation behavior of titratable groups in proteins. Based on the coordinates of the Paracoccus denitrificans cytochrome c oxidase, we have determined the electrostatic potential in and around the protein, calculated the titration curves for all ionizable residues in the protein, and analyzed the response of the protein environment to redox changes at the metal centers. The results of this study provide insight into how charged groups can be stabilized within a low-dielectric environment and how the range of their electrostatic effects can be modulated by the protein. A cluster of 18 titratable groups around the heme a 3–CuB binuclear center, including a hydroxide ion bound to the copper, was identified that accounts for most of the proton uptake associated with redox changes at the binuclear site. Predicted changes in net protonation were in reasonable agreement with experimentally determined values. The relevance of these findings in the light of possible mechanisms of redox-coupled proton movement is discussed.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1023/A:1020563629032
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  • 2
    Digitale Medien
    Digitale Medien
    Crystals of an antibody FV fragment against an integral membrane protein diffracting to 1.28 Å resolution (1995)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 21 (1995), S. 74-77 
    Details
    ISSN: 0887-3585
    Schlagwort(e): crystallization ; membrane protein ; X-ray diffraction ; atomic resolution ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: The Fv fragment of a monoclonal antibody, 7E2 (IgG1, κ, murine), which is directed against the integral membrane protein cytochrome c oxidase (EC 1.9.3.1) from Paracoccus denitrificans, was cloned and produced in Escherichia coli. Crystals suitable for highresolution X-ray analysis were obtained by microdialysis under low salt conditions. The crystals belong to the orthorhombic space group P212121 with unit cell dimensions of a = 51.51 Å, b = 56.15 Å, c = 99.86 Å (1 Å = 0.1 nm) and contain one F v fragment per asymmetric unit. Using synchrotron radiation diffraction data were collected up to 1.28 Å resolution. This high resolution is very unusual for a heterodimeric protein. The crystals should open the way for refining not only the atomic positions, but also for obtaining information about internal dynamics. © 1995 Wiley-Liss, Inc.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/prot.340210110
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  • 3
    Digitale Medien
    Digitale Medien
    Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 26 (1996), S. 118-120 
    Details
    ISSN: 0887-3585
    Schlagwort(e): Protein crystallization ; X-ray crystallography ; methanogenic Archaea ; hyperthermophilic enzymes ; halophilic enzymes ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: Formylmethanofuran:tetrahydromethanopterin formyltransferase from the hyperthermophilic methanogenic Archaeon Methanopyrus kandleri (growth temperature optimum 98°C) was crystallized by vapor diffusion methods. Crystal form M obtained with 2-methyl-2,4-pentanediol as precipitant displayed the space group P21 with unit cell parameters of a = 87.0 Å, b = 75.4 Å, c = 104.7 Å, and β = 113.9° and diffracted better than 2 Å resolution. Crystal form P grown from polyethylene glycol 8000 belonged to the space group I4122 and had unit cell parameters of 157.5 Å and 242.1 Å. Diffraction data to 1.73 Å were recorded. Crystal form S which was crystallized from (NH4)2SO4in the space group I4122 with unit cell parameters of 151.3 Å and 249.5 Å diffracted at least to 2.2 Å resolution. All crystal forms probably have four molecules per asymmetric unit and are suitable for X-ray structure analysis. © 1996 Wiley-Liss, Inc.
    Materialart: Digitale Medien
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  • 4
    Digitale Medien
    Digitale Medien
    Das photosynthetische Reaktionszentrum des Purpurbakteriums Rhodopseudomonas viridis (Nobel-Vortrag)Copyright © The Nobel Foundation 1989. - Wir danken der Nobel-Stiftung, Stockholm, für die Genehmigung zum Druck einer deutschen Fassung des Vortrags. (1989)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 101 (1989), S. 872-892 
    Details
    ISSN: 0044-8249
    Schlagwort(e): Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: In unseren Vorträgen beschrieben wir zunächst die Geschichte und die Methoden der Kristallisation von Membranproteinen. Dann zeigen wir, wie die Struktur des photosynthetischen Reaktionszentrums aus dem Purpurbakterium Rhodopseudomonas viridis bestimmt wurde. Danach wird die Struktur dieses Membranprotein-Komplexes mit seiner Funktion als lichtegetriebene Elektronenpumpe über die photosynthetische Membran korreliert. Schließlich ziehen wir Rückschlüsse auf die Struktur des Reaktionszentrums des Photosystems II der Pflanze und diskutieren die spezifischen Gesichtspunkte der Membranprotein-Struktur. Die Abschnitte 1 (Kristallisation), 4 (Verwandtschaft mit dem Photosystem II und evolutionäre Aspekte) und 5 (Membranprotein-Struktur) wurden von H. M. im Vortrag präsentiert und verfaßt, die Abschnitte 2 (Strukturaufklärung) und 3 (Struktur und Funktion) von J. D. Wir Wählen diese Anordnung, um dem Leser das Verständnis des Zusammenhangs zu erleichtern.
    Zusätzliches Material: 23 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/ange.19891010705
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  • 5
    Digitale Medien
    Digitale Medien
    The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis (Nobel Lecture)Copyright © The Nobel Foundation 1989. - We thank the Nobel Foundation, Stockholm, for permission to print this lecture. (1989)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 28 (1989), S. 829-847 
    Details
    ISSN: 0570-0833
    Schlagwort(e): Purple bacterium ; Nobel lecture ; Photosynthesis ; X-ray structure analysis ; Proteins ; Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: In our lecture we first describe the history and methods of membrane protein crystallization, before we show how the structure of the photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis was solved. The structure of this membrane protein complex is then correlated with its function as a light-driven electron pump across the photosynthetic membrane. Finally, we draw conclusions on the structure of the photosystem II reaciton center of plants and discuss the aspects of membrane protein structure. Sections 1 (crystallization), 4 (conclusions on the structure of photosystem II reaction center and evolutionary aspects) and 5 (aspects of membrane protein structure) were presented and written by H. M., sections 2 (determination of the structure) and 3 (structure and function) by J. D. We have arranged the manuscript in this way in order to facilitate continuous reading.
    Zusätzliches Material: 23 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/anie.198908293
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