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Structure of amyloid aggregates of lysozyme from small-angle X-ray scattering data
Authors:V. I. Petrenko  M. V. Avdeev  V. M. Garamus  M. Kubovcikova  Z. Gažová  K. Šipošová  L. A. Bulavin  L. Almásy  V. L. Aksenov  P. Kopcansky
Affiliation:1. Joint Institute for Nuclear Research, ul. Joliot-Curie 6, Dubna, Moscow oblast, 141980, Russia
2. Taras Shevchenko National University of Kyiv, ul. Volodymyrska 60, Kyiv, 01601, Ukraine
3. Helmholtz-Zentrum Geesthacht, Max-Planck-Stra?e 1, Geesthacht, 21502, Germany
4. Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, Ko?ice, 040 01, Slovakia
5. Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences, 29-33 Konkoly-Thege M. Street, Budapest, Hungary
6. Konstantinov Petersburg Nuclear Physics Institute, National Research Centre “Kurchatov Institute,” Orlova Roshcha, Gatchina, Leningrad oblast, 188300, Russia
Abstract:The structure of filament amyloid aggregates of hen egg white lysozyme in water has been investigated by the small-angle X-ray scattering method. The experimental data are described by different cylindrical models, among which the best agreement is reached with the long helix model. A comparison of the results with the small-angle neutron scattering data reveals the influence of the heavy component of the solvent (a H2O/D2O mixture) on the structure of the filaments.
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