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. 2000 Apr;78(4):2180–2185. doi: 10.1016/S0006-3495(00)76765-8

F-actin retains a memory of angular order.

A Orlova 1, E H Egelman 1
PMCID: PMC1300810  PMID: 10733996

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.

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Selected References

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