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Fibrous Proteins: Structures and Mechanisms

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Attention for Chapter 5: Fibrous Proteins: Structures and Mechanisms
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Chapter title
Fibrous Proteins: Structures and Mechanisms
Chapter number 5
Book title
Fibrous Proteins: Structures and Mechanisms
Published in
Sub cellular biochemistry, January 2017
DOI 10.1007/978-3-319-49674-0_5
Pubmed ID
Book ISBNs
978-3-31-949672-6, 978-3-31-949674-0
Authors

Fraser, R. D. Bruce, Parry, David A. D., R. D. Bruce Fraser, David A. D. Parry

Abstract

The intermediate filaments (IF) in trichocyte (hard α-) keratin are unique amongst the various classes of IF in having not one but two topologically-distinct structures. The first is formed at an early stage of hair development in a reducing environment within the cells in the lower part of the follicle. The second structure occurs at a later stage of hair development in the upper part of the follicle, where there is a transition to an oxidizing environment. Crosslinking studies reveal that molecular slippage occurs within the IF upon oxidation and that this results in many cysteine residues lying in near axial alignment, thereby facilitating disulphide bond formation. The disulphide bonds so formed stabilize the assembly of IF molecules and convert the keratin fibre into a tough, resilient and insoluble structure suitable for its function in vivo as a thermo-regulator and a protector of the animal against its external environment.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 7 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 7 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 2 29%
Student > Bachelor 1 14%
Student > Doctoral Student 1 14%
Student > Master 1 14%
Unknown 2 29%
Readers by discipline Count As %
Mathematics 2 29%
Biochemistry, Genetics and Molecular Biology 1 14%
Business, Management and Accounting 1 14%
Unknown 3 43%