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. 1979 Aug;76(8):3857–3859. doi: 10.1073/pnas.76.8.3857

On the molecular basis for chemomechanical energy transduction in muscle.

M F Morales, J Botts
PMCID: PMC383934  PMID: 291046

Abstract

Herein it is developed that energy transduction in muscle is an activity of myosin S-1 and its ligands, actin (A) and nucleotide (N). S-1 shares with other molecular particles (e.g., hemoglobin) the property that binding events at one of its sites, the N-site, influences binding events at a remote site, the A site (specifically, influences both the actin affinity and actin attachment angle at the A site). However, there is a crucial difference between S-1 and the better-known systems. Because the N site is enzymatic, it has a temporal sequence of occupants; this imposes a temporal sequence of actin attitudes--i.e., a sequence of mechanical events.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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