Myosin of the non-motile stereocilia located in the inner ear. It is thought to be functional as a monomer. Note that not all of these genes are active. Myosin light chains are distinct and have their own properties. They are not considered "myosins" but are components of the macromolecular complexes that make up the functional myosin enzymes. Paramyosin is a large, 93-115kDa muscle protein that has been described in a number of diverse invertebrate phyla. Invertebrate thick filaments are thought to be composed of an inner paramyosin core surrounded by myosin. The myosin interacts with actin, resulting in fibre contraction. Paramyosin
Alpha-keratin of most biological importance of alpha-keratin is its structural stability. When exposed to mechanical stress, α-keratin structures can retain their shape and therefore can protect what they surround. Under high tension, alpha-keratin can even change into beta-keratin, a stronger keratin formation that has a secondary structure of beta-pleated sheets. Alpha-keratin tissues also show signs of viscoelasticity, allowing them to both be able to stretch and absorb impact to a degree, though they are not impervious to fracture. Alpha-keratin strength is also affected by water content in the intermediate filament matrix; higher water content decreases the strength and stiffness of the