X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS | Zendy

E. D. Eanes | Zendy; G. G. Glenner | Zendy

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X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS

Author(s) -

E. D. Eanes,

G. G. Glenner

Publication year - 1968

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/16.11.673

Subject(s) - antiparallel (mathematics) , protein filament , crystallography , diffraction , amyloid (mycology) , folding (dsp implementation) , amyloid fibril , fiber diffraction , x ray crystallography , x ray , materials science , chemistry , biophysics , amyloid β , optics , physics , biology , pathology , composite material , medicine , inorganic chemistry , disease , electrical engineering , quantum mechanics , magnetic field , engineering

The filamentous protein component of amyloid-laden tissue was studied by x-ray diffraction procedures. The principal features of the x-ray pattern from nonoriented amyloid material consist of a sharp, intense ring at 4.75 Å overlaying a diffuse halo at 4.3 Å, and a broad and less intense ring at 9.8 Å. When oriented, the material gives a "cross-β" x-ray pattern. The x-ray findings are interpreted in terms of a "pleated sheet" structure formed by the amyloid polypeptide chain folding in a regular manner on itself such that adjacent chain segments are laterally arranged in an antiparallel manner. The x-ray patterns from oriented amyloid suggest further that the axes of the chain segments run transverse to the filament axis.

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