▪ Abstract X-ray crystallography shows the myosin cross-bridge to exist in two conformations,
the beginning and end of the “power stroke.” A long lever-arm undergoes a 60° to 70° …

The myosin cross–bridge exists in two conformations, which differ in the orientation of a long
lever arm. Since the lever arm undergoes a 60° rotation between the two conformations …

The interaction of myosin with actin filaments is the central feature of muscle contraction and
cargo movement along actin filaments of the cytoskeleton. The energy for these movements …

The function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is
activated during polymerization; a delay between hydrolysis and inorganic phosphate (Pi) …

The crystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD)
and a motor domain–essential light chain (ELC) complex (MDE), both with a transition state …

This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

The crystal structure of a proteolytic subfragment from scallop striated muscle myosin,
complexed with MgADP, has been solved at 2.5 Å resolution and reveals an unusual …

We have determined the structure of the intact scallop myosin head, containing both the
motor domain and the lever arm, in the nucleotide-free state and in the presence of …

Omecamtiv Mecarbil (OM) is a small molecule allosteric effector of cardiac myosin that is in
clinical trials for treatment of systolic heart failure. A detailed kinetic analysis of cardiac …

During skeletal muscle contraction, regular arrays of actin and myosin filaments slide past
each other driven by the cyclic ATP-dependent interaction of the motor protein myosin II (the …