Literature DB >> 128756

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

T L Hill, R M Simmons.   

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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Year:  1976        PMID: 128756      PMCID: PMC335902          DOI: 10.1073/pnas.73.2.336

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  4 in total

1.  Free energy levels and entropy production associated with biochemical kinetic diagrams.

Authors:  T L Hill; R M Simmons
Journal:  Proc Natl Acad Sci U S A       Date:  1976-01       Impact factor: 11.205

2.  Theoretical formalism for the sliding filament model of contraction of striated muscle. Part II.

Authors:  T L Hill
Journal:  Prog Biophys Mol Biol       Date:  1975       Impact factor: 3.667

Review 3.  Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I.

Authors:  T L Hill
Journal:  Prog Biophys Mol Biol       Date:  1974       Impact factor: 3.667

4.  Mechanism of adenosine triphosphate hydrolysis by actomyosin.

Authors:  R W Lymn; E W Taylor
Journal:  Biochemistry       Date:  1971-12-07       Impact factor: 3.162

  4 in total
  2 in total

1.  Steady-state kinetic formalism applied to multienzyme complexes, oxidative phosphorylation, and interacting enzymes.

Authors:  T L Hill
Journal:  Proc Natl Acad Sci U S A       Date:  1976-12       Impact factor: 11.205

Review 2.  The mechanochemistry of force production in muscle.

Authors:  H J Kuhn
Journal:  J Muscle Res Cell Motil       Date:  1981-03       Impact factor: 2.698

  2 in total

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