Key result
Actin retains its paracrystalline conformation by EPR in morphologically non-paracrystalline states, indicating the P state is a distinct molecular conformation required for bundle formation.
Population
Rabbit muscle actin
Design
Preclinical
Authors
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Actin P-state conformation may guide bundle assembly in models; leaves open relevance to cardiac cytoskeletal function.
The paracrystalline state of actin is a distinct molecular conformation required for actin monomers to aggregate into bundles and paracrystals.
Harwell et al. (1980) studied this question. MgCl2, KCl, DNase I, cytochalasin B, and phalloidin was evaluated on Conformation changes of actin measured by EPR and electron microscopy. Actin retains its paracrystalline conformation by EPR in morphologically non-paracrystalline states, indicating the P state is a distinct molecular conformation required for bundle formation.
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