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Title: The Molecular Architecture for the Intermediate Filaments of Hard α -Keratin Based on the Superlattice Data Obtained from a Study of Mammals Using Synchrotron Fibre Diffraction

High- and low-angle X-ray diffraction studies of hard α -keratin have been studied, and various models have been proposed over the last 70 years. Most of these studies have been confined to one or two forms of alpha keratin. This high- and low-angle synchrotron fibre diffraction study extends the study to cover all available data for all known forms of hard α -keratin including hairs, fingernails, hooves, horn, and quills from mammals, marsupials, and a monotreme, and it confirms that the model proposed is universally acceptable for all mammals. A complete Bragg analysis of the meridional diffraction patterns, including multiple-time exposures to verify any weak reflections, verified the existence of a superlattice consisting of two infinite lattices and three finite lattices. An analysis of the equatorial patterns establishes the radii of the oligomeric levels of dimers, tetramers, and intermediate filaments (IFs) together with the centre to centre distance for the IFs, thus confirming the proposed helices within helices molecular architecture for hard α -keratin. The results verify that the structure proposed by Feughelman and James meets the criteria for a valid α -keratin structure.
Authors:
 [1]
  1. Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia
Publication Date:
OSTI Identifier:
1198197
Grant/Contract Number:
W-31-109-ENG-38
Type:
Published Article
Journal Name:
Biochemistry Research International
Additional Journal Information:
Journal Volume: 2011; Related Information: CHORUS Timestamp: 2016-08-04 08:36:00; Journal ID: ISSN 2090-2247
Publisher:
Hindawi Publishing Corporation
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
Country unknown/Code not available
Language:
English