F-actin retains a memory of angular order.

Abstract

Modifications can be made to F-actin that do not interfere with the binding of myosin but inhibit force generation, suggesting that actin's internal dynamics are important for muscle contraction. Observations from electron microscopy and x-ray diffraction have shown that subunits in F-actin have a relatively fixed axial rise but a variable twist. One possible explanation for this is that the actin subunits randomly exist in different discrete states of "twist, " with a significant energy barrier separating these states. This would result in very slow torsional transitions. Paracrystals impose increased order on F-actin filaments by reducing the variability in twist. By looking at filaments that have recently been dissociated from paracrystals, we find that F-actin retains a "memory" of its previous environment that persists for many seconds. This would be consistent with slow torsional transitions between discrete states of twist.