Abstract
Myosin filaments of muscle are regulated either by phosphorylation of their regulatory light chains or Ca2+-binding to the essential light chains, contributing to on-off switching or modulation of contraction. Phosphorylation-regulated filaments in the relaxed state are characterized by an asymmetric interaction between the “blocked” and “free” heads of each myosin, inhibiting actin-binding or ATPase activity (Wendt et al., 2001; Woodhead et al., 2005). We have tested whether a similar interaction occurs in Ca2+-regulated filaments.
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