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
Author
Source
Biochemistry Research International
Issue
Vol. 2011, Issue 2011 (31 Dec. 2011), pp.1-10, 10 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2011-10-19
Country of Publication
Egypt
No. of Pages
10
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
James, Veronica. 2011. 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. Biochemistry Research International،Vol. 2011, no. 2011, pp.1-10.
https://search.emarefa.net/detail/BIM-453875
Modern Language Association (MLA)
James, Veronica. 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. Biochemistry Research International No. 2011 (2011), pp.1-10.
https://search.emarefa.net/detail/BIM-453875
American Medical Association (AMA)
James, Veronica. 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. Biochemistry Research International. 2011. Vol. 2011, no. 2011, pp.1-10.
https://search.emarefa.net/detail/BIM-453875
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-453875