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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Feb;73(2):336–340. doi: 10.1073/pnas.73.2.336

Free energy levels and entropy production in muscle contraction and in related solution systems.

T L Hill, R M Simmons
PMCID: PMC335902  PMID: 128756

Abstract

"Basic" and "gross" free energy levels of a macromolecule such as myosin or Na,K-ATPase, defined in a previous publication, are discussed here for two relatively complicated cases: a six-state kinetic diagram of the sort that could be used to describe the actin activation of myosin-ATPase in solution; and muscle contraction, where a similar kinetic diagram is needed for each value of a positional variable X.

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Selected References

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

  1. Hill T. L., Simmons R. M. Free energy levels and entropy production associated with biochemical kinetic diagrams. Proc Natl Acad Sci U S A. 1976 Jan;73(1):95–99. doi: 10.1073/pnas.73.1.95. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Hill T. L. Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I. Prog Biophys Mol Biol. 1974;28:267–340. doi: 10.1016/0079-6107(74)90020-0. [DOI] [PubMed] [Google Scholar]
  3. Hill T. L. Theoretical formalism for the sliding filament model of contraction of striated muscle. Part II. Prog Biophys Mol Biol. 1975;29(2):105–159. doi: 10.1016/0079-6107(76)90021-3. [DOI] [PubMed] [Google Scholar]
  4. Lymn R. W., Taylor E. W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 1971 Dec 7;10(25):4617–4624. doi: 10.1021/bi00801a004. [DOI] [PubMed] [Google Scholar]

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