Motors, molecular protein, actin-binding

The 20-amino acid residue peptide RS-20, whose sequence derives from smooth muscle myosin light chain kinase (MLCK), is a well-known calmodulin binding peptide [144], Both, RS-20 and LMS-1, a 13-residue peptide derived from the autoinhibitory domain of MLCK, have the capability of inhibiting MLCK phosphorylation activity, normally directed toward the molecular motor, actin binding protein myosin II, which is involved in physiological phenomena like cell polarization and locomotion [145, 146]. 

The horse, like all animals, is powered by the molecular motor protein, myosin. A portion of myosin moves dramatically (as shown above) in response to ATP binding, hydrolysis, and release, propelling myosin along an actin filament. This molecular movement is translated into movement of the entire animal, excitingly depicted in da Vinci s rearing horse. [(Left) Leonardo da Vinci s "Study of a rearing horse" for the battle of Anghiari (c. 1504) from The Royal Collection Her Royal Majesty Queen Elizabeth II.]... 

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