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Filamentous Supramolecular Structures
Author(s) -
Burchard Walther
Publication year - 2010
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.201000004
Subject(s) - radius of gyration , protein filament , molar mass , supramolecular chemistry , crystallography , scattering , amyloid (mycology) , helix (gastropod) , bundle , small angle x ray scattering , chemistry , chemical physics , light scattering , radius , materials science , physics , polymer , optics , composite material , organic chemistry , biology , crystal structure , snail , inorganic chemistry , ecology , computer security , computer science
Summary: The formation of four filament forming proteins was studied mainly by light scattering as a function of the scattering angle. Besides the molar mass M w and the radius of gyration R g the contour length L , was determined. The corresponding structure parameters are compared with those of the A β ‐amyloid. A minimum cross‐sectional diameter of 2 nm appeared to be necessary for filament stabilization. Bundle and network formation are often observed and are tentatively explained by thermodynamic arguments. The local conformation of the unimer proteins in the filaments remained largely unexplored. Only in one example CD and IR spectroscopy was applied. The analysis disclosed a β‐ sheet/ α ‐helix transition on de‐naturation, as was conjectured before as reason for the A β ‐amyloid formation.