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PMID: 12033398 Published · ppublish English Journal Article

The structure of the alpha-keratin microfibril.

Bioscience reports ·Vol. 3 ·No. 6 ·1983-06-00 ·Pages 517-25

Fraser RD, MacRae TP

Abstract

Quantitative measurements of the intensity of the meridional reflections in the X-ray-diffraction pattern of alpha-keratin are shown to be consistent with a microfibril structure in which a surface lattice with an axially projected period around 200 A is subject to a periodic interruption with an axially projected period of 470 A. Taken in conjunction with recent evidence on the chemical structure of alpha-keratin and other intermediate filaments this finding enables an elaboration to be made of a model proposed earlier by RDB Fraser, TP MacRae, & E Suzuki (J. Mol. Biol. 108, 435-452, 1976) for the alpha-helical framework of the microfibril. The disposition and connectivity of the helical segments suggested here provides a straightforward explanation of a number of recent physicochemical and electron-microscopical observations on intermediate filaments and provides a starting point for the development of models for the framework of other intermediate filaments.

MeSH Terms
Keratins/chemistry Microfibrils/chemistry Models, Structural Protein Conformation Protein Structure, Secondary X-Ray Diffraction
Chemicals
Keratins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fraser R D
Division of Protein Chemistry, CSIRO, Parkville, Victoria, Australia.
MacRae T P
Article Info
Journal
Bioscience reports
Abbr.
Biosci Rep
ISSN
0144-8463
Published
1983-06-00
Pages
517-25
Language
English
Region
England
NLM ID
8102797
Subset
IM
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