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  • 1
    Language: English
    In: ChemPhysChem, 22 December 2008, Vol.9(18), pp.2809-2815
    Description: Herein, we explore the effect of different types of osmolytes on the high‐pressure stability and tertiary structure of a well‐characterized monomeric protein, staphylococcal nuclease (SNase). Changes in the denaturation pressure and the radius of gyration are obtained in the presence of different concentrations of trimethylamine N‐oxide (TMAO), glycerol and urea. To reveal structural changes in the protein upon compression at various osmolyte conditions, small‐angle X‐ray scattering (SAXS) experiments were carried out. To this end, a new high‐pressure cell suitable for high‐precision SAXS studies at synchrotron sources was built, which allows one to carry out scattering experiments up to maximum pressures of about 7 kbar. Our data clearly indicate that the osmolytes that stabilize proteins against temperature‐induced unfolding drastically increase their pressure stability and that the elliptically shaped curve of the pressure–temperature–stability diagram of proteins is shifted to higher temperatures and pressures with increasing osmolyte concentration. A drastic stabilization is observed for the osmolyte TMAO, which exhibits not only a significant stabilization against temperature‐induced unfolding, but also a particularly strong stabilization of the protein against pressure. In fact, such findings are in accordance with in vivo studies (for example P. J. Yancey, , , 2819–2830), where unusually high TMAO concentrations in some deep‐sea animals were found. Conversely, chaotropic agents such as urea have a strong destabilizing effect on both the temperature and pressure stability of the protein. Our data also indicate that sufficiently high TMAO concentrations might be able to largely offset the destabilizing effect of urea. The different scenarios observed are discussed in the context of recent experimental and theoretical studies. The high‐pressure denaturation (see picture of the custom‐built sample cell) of proteins is studied in the presence of different osmolytes and compared to temperature‐induced unfolding. The osmolytes that stabilize proteins against temperature‐induced unfolding also increase their pressure stability. Significant stabilizing effects are seen for glycerol and trimethylamine N‐oxide.
    Keywords: Cosolvents ; High‐Pressure Chemistry ; Osmolytes ; Proteins ; Small‐Angle X‐Ray Scattering
    ISSN: 1439-4235
    E-ISSN: 1439-7641
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  • 2
    Language: English
    In: Journal of synchrotron radiation, May 2007, Vol.14(Pt 3), pp.244-51
    Description: The multi-purpose experimental endstation of beamline BL9 at the Dortmund Electron Accelerator (DELTA) is dedicated to diffraction experiments in grazing-incidence geometry, reflectivity and powder diffraction measurements. Moreover, fluorescence analysis and inelastic X-ray scattering experiments can be performed. Recently, a new set-up for small-angle and wide-angle X-ray scattering utilizing detection by means of an image-plate scanner was installed and is described in detail here. First small-angle X-ray scattering experiments on aqueous solutions of lysozyme with different cosolvents and of staphylococcal nuclease are discussed. The application of the set-up for texture analysis is emphasized and a study of the crystallographic texture of natural bio-nanocomposites, using lobster and crab cuticles as model materials, is presented.
    Keywords: X-Ray Diffraction -- Instrumentation
    ISSN: 0909-0495
    E-ISSN: 16005775
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  • 3
    In: Journal of Synchrotron Radiation, May 2007, Vol.14(3), pp.244-251
    Description: The multi‐purpose experimental endstation of beamline BL9 at the Dortmund Electron Accelerator (DELTA) is dedicated to diffraction experiments in grazing‐incidence geometry, reflectivity and powder diffraction measurements. Moreover, fluorescence analysis and inelastic X‐ray scattering experiments can be performed. Recently, a new set‐up for small‐angle and wide‐angle X‐ray scattering utilizing detection by means of an image‐plate scanner was installed and is described in detail here. First small‐angle X‐ray scattering experiments on aqueous solutions of lysozyme with different cosolvents and of staphylococcal nuclease are discussed. The application of the set‐up for texture analysis is emphasized and a study of the crystallographic texture of natural bio‐nanocomposites, using lobster and crab cuticles as model materials, is presented.
    Keywords: Saxs ; Waxs ; Solution Scattering ; Texture Analysis ; Protein ; Lysozyme ; X‐Ray Diffraction.
    ISSN: 0909-0495
    E-ISSN: 1600-5775
    Source: John Wiley & Sons, Inc.
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  • 4
    In: Journal of Synchrotron Radiation, 07/2007, Vol.14(4), pp.391-391
    Description: To purchase or authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1107/S0909049507020729 Abstract: A correction is made to the equation in Krywka et al. (2007), J. Synchrotron Rad.14, 244-251 . Author Affiliation: (a)Department of Physics, DELTA, University of Dortmund, D-44221 Dortmund, Germany (b)Department of Chemistry, University of Dortmund, D-44221 Dortmund, Germany (c)Max-Planck-Institut fur Eisenforschung, D-40237 Dusseldorf, Germany (d)TU Clausthal, Institut fur Werkstoffkunde und Werkstofftechnik, D-38678 Clausthal-Zellerfeld, Germany Article History: Received 19 April 2007, accepted 19 April 2007 Article note: Christina Krywka, e-mail: krywka@physik.uni-dortmund.de
    ISSN: 0909-0495
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  • 5
    In: Journal of Synchrotron Radiation, July 2007, Vol.14(4), pp.391-391
    Description: A correction is made to the equation in Krywka .
    ISSN: 0909-0495
    E-ISSN: 1600-5775
    Source: John Wiley & Sons, Inc.
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  • 6
    Language: English
    In: ChemPhysChem, 12/22/2008, Vol.9(18), pp.2633-2633
    Description: The cover picture shows water molecules in different hydration shells at the surface of the model protein ubiquitin. The properties of proteins and the role of solvent in conformational dynamics is a central topic to the DFG‐Foschergruppe (FOR 436) which forms the basis of this special issue. The polymorphism, dynamics and function of water at molecular interfaces is discussed with contributions from R. Winter (p. 2715, 2779), Ludwig (p. 2722, 2731), Geiger and Paschek (p. 2722, 2737, 2742), Brovchenko ( p. 2660, 2695), Tolan (p. 2809), Marx ( p. 2703, 2751, 2759 ), and Weingärtner ( p. 2794, 2802).
    Keywords: Chemistry;
    ISSN: ChemPhysChem
    E-ISSN: 14394235
    E-ISSN: 14397641
    Source: Wiley (via CrossRef)
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