DOI: 10.1177/16.11.673. X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS

X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS

10.1177/16.11.673

Crossref journal-article

SAGE Publications

Journal of Histochemistry & Cytochemistry (179)

Abstract

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.

Bibliography

EANES, E. D., & GLENNER, G. G. (1968). X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS. Journal of Histochemistry & Cytochemistry, 16(11), 673â677.

Authors 2

E. D. EANES (first)
G. G. GLENNER (additional)

References 0 Referenced 665

None

Dates

Type	When
Created	14 years, 4 months ago (April 1, 2011, 12:54 a.m.)
Deposited	5 months, 3 weeks ago (March 1, 2025, 10:58 p.m.)
Indexed	5 days, 9 hours ago (Aug. 19, 2025, 6:26 a.m.)
Issued	56 years, 9 months ago (Nov. 1, 1968)
Published	56 years, 9 months ago (Nov. 1, 1968)
Published Online	56 years, 9 months ago (Nov. 1, 1968)
Published Print	56 years, 9 months ago (Nov. 1, 1968)

Funders 0

None

BibTeX

@article{EANES_1968, title={X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS}, volume={16}, ISSN={1551-5044}, url={http://dx.doi.org/10.1177/16.11.673}, DOI={10.1177/16.11.673}, number={11}, journal={Journal of Histochemistry & Cytochemistry}, publisher={SAGE Publications}, author={EANES, E. D. and GLENNER, G. G.}, year={1968}, month=nov, pages={673–677} }

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