Myosin II is a molecular motor that converts chemical energy derived from ATP hydrolysis
into mechanical work. Myosin II isoforms are responsible for muscle contraction and a range …

The heart is an extraordinarily versatile pump, finely tuned to respond to a multitude of
demands. Given the heart pumps without rest for decades its efficiency is particularly …

Every heartbeat relies on cyclical interactions between myosin thick and actin thin filaments
orchestrated by rising and falling Ca2+ levels. Thin filaments are comprised of two actin …

We develop a point model of the cardiac myofilament (MF) to simulate a wide variety of
experimental muscle characterizations including Force-Ca relations and twitches under …

Understanding the dynamics of a cardiac muscle twitch contraction is complex because it
requires a detailed understanding of the kinetic processes of the Ca 2+ transient, thin …

Cardiac muscle contraction is distinct from the contraction of other muscle types. The heart
continuously undergoes contraction–relaxation cycles throughout an animal's lifespan. It …

In muscle, force emerges from myosin binding with actin (forming a cross-bridge). This
actomyosin binding depends upon myofilament geometry, kinetics of thin-filament Ca2+ …

The effect of molecule tethering in three-dimensional (3-D) space on bimolecular binding
kinetics is rarely addressed and only occasionally incorporated into models of cell motility …

Muscles produce force and power by utilizing chemical energy through ATP hydrolysis.
During concentric contractions (shortening), muscles generate less force compared to …

We studied the effect of titin-based passive tension on sarcomere structure by
simultaneously measuring passive tension and low-angle x-ray diffraction patterns on …