The role of β-sheets in the structure and assembly of keratins

Biophysics Reviews
R D FRASER, D A Parry

Abstract

X-ray diffraction, infrared and electron microscope studies of avian and reptilian keratins, and of stretched wool and hair, have played a central role in the development of models for the β-conformation in proteins. Both α- and β-keratins contain sequences that are predicted to adopt a β-conformation and these are believed to play an important part in the assembly of the filaments and in determining their mechanical properties. Interactions between the small β-sheets in keratins provide a simple mechanism through which shape and chemical complementarity can mediate the assembly of molecules into highly specific structures. Interacting β-sheets in crystalline proteins are often related to one another by diad symmetry and the data available on feather keratin suggest that the filament is assembled from dimers in which the β-sheets are related by a perpendicular diad. The most detailed model currently available is for feather and reptilian keratin but the presence of related β-structural forms in mammalian keratins is also noted.

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Citations

Jan 15, 2019·Journal of Experimental Zoology. Part B, Molecular and Developmental Evolution·Karin Brigit HolthausLorenzo Alibardi
Aug 11, 2016·Journal of Experimental Zoology. Part B, Molecular and Developmental Evolution·Lorenzo Alibardi
Aug 10, 2020·Biotechnology Advances·Jingwen QiuAnne S Meyer
Feb 2, 2018·The Journal of Physical Chemistry. B·Kenkoh S EndohFlorian Müller-Plathe

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