The myosin 2 family of molecular motors includes isoforms regulated in different ways. Vertebrate smooth-muscle myosin is activated by phosphorylation of the regulatory light chain, whereas scallop ...

Conformational changes within myosin lead to its movement relative to an actin filament. Several crystal structures exist for myosin bound to various nucleotides, but none with bound actin. Therefore, ...

Muscle contraction involves the cyclic interaction of the myosin cross-bridges with the actin filament, which is coupled to steps in the hydrolysis of ATP 1. While bound to actin each cross-bridge ...

The results discussed in the preceding paper indicate that A-band shortening in Limulus muscle is a thick filament response to activation that occurs largely by fragmentation of filament ends. To ...

After five years of work, a team from National Biosciences Laboratory (LNBio), in the city of Campinas, has defined the three-dimensional structure of what is called the functional, or active, region ...

A team of Yale and University of Pennsylvania researchers recently discovered that myosin, one of the proteins responsible for muscle contraction, can sense and adapt to different amounts of force.

Researchers have characterised changes in the structure of motor proteins, called myosins, and energy consumption that occur during hibernation, highlighting key differences in large and small ...

image: This graphic shows the proposed binding site for omecamtiv mecarbil to cardiac myosin S1. The ribbon diagram to the left shows the major features of the myosin S1 head. A spacefilling model of ...

Researchers have shed light on the molecular mechanisms underlying hibernation, publishing their findings today as a Reviewed Preprint in eLife. Their research, in small and large hibernating mammals, ...

Cells use the polymerization of actin alone to create some types of movement, but many other forms of movement require interplay between actin and an enzyme called ...