Many motile bacteria have rotating fiber (flagellum) generating from a cell surface which functions like a screw and create a driving force to move or swim.
At the proximal end of flagellum there is a rotary motor which is composed of a rotor and a stator and ions, Na or H , flow into cells by way of the stator.
Such research should lead to the clarification of the molecular mechanisms underlying the pathologic lesions observed in the tissues and organs of patients with chaperonopathies.
Information on these key issues is necessary to make progress in diagnosis and treatment.
The mechanical response of α-keratin has been extensively studied and shows linear Hookean, yield and post-yield regions, and in some cases, a high reversible elastic deformation.
A ubiquitous biological material, keratin represents a group of insoluble, usually high-sulfur content and filament-forming proteins, constituting the bulk of epidermal appendages such as hair, nails, claws, turtle scutes, horns, whale baleen, beaks, and feathers.
These keratinous materials are formed by cells filled with keratin and are considered ‘dead tissues’.
Researchers used biochemical techniques and electron microscopy to uncover the structure of the bacterial Mot A protein, which forms part of the propeller motor (flagellum).
Three-dimensional analysis found it is composed of a transmembrane component and cytoplasmic domain, while Mot A molecules were shown to form stable tetramer complexes with other Mot A molecules.