The catalytic head of myosin is a globular structure that has historically
been divided into three segments of 25, 50, and 20 kDa. The solvent-exposed
, proteolytically-sensitive surface loops of myosin that join these three s
egments are highly variable in their sequences. While surface loops have no
t traditionally been thought to affect enzymatic activities, these loops li
e near the ATP and actin-binding sites and have been implicated in the modu
lation of myosin's kinetic activities. In this work we review the wealth of
data regarding the loops that has accumulated over the years and discuss t
he roles of the loops in contributing to the different activities displayed
by different myosin isoforms.