The structure of the α-keratin microfibril

Author:

Fraser R. D. B.1,MacRae T. P.1

Affiliation:

1. Division of Protein Chemistry, CSIRO, 343 Royal Parade, Parkville, Victoria 3052, Australia

Abstract

Quantitative measurements of the intensity of the meridional reflections in the X-ray-diffraction pattern of α-keratin are shown to be consistent with a microfibril structure in which a surface lattice with an axially projected period around 200 Å is subject to a periodic interruption with an axially projected period of 470 Å. Taken in conjunction with recent evidence on the chemical structure of α-keratin and other inter-mediate filaments this finding enables an elaboration to be made of a model proposed earlier by RDB Fraser, TP MacRae, & E Suzuki (3. Mol. Biol. 108, 435–452, 1976.) for the α-helical framework of the microfibrii. 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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference34 articles.

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2. Bear RS (1944) J. Amer. Chem. Soc.66, 2043?2050.

3. Birbeck MSC & Mercer EH (1957) J. Biophys. Biochem. Cytol.3, 203?214.

4. Crewther WG & Dowling LM (1971) Applied Polymer Symp.18, 1?20.

5. Crewther WG, Dowling LM, Gruen LC, Sparrow LG & Woods EF (1980a) Proc. Int. Wool Text. Res. Conf., 6th, Pretoria,2, 1?12.

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