Open AccessFree energy levels and entropy production in muscle contraction and in related solution systems.
Author(s) -
Terrell L. Hill,
Robert Simmons
Publication year - 1976
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.73.2.336
Subject(s) - myosin , kinetic energy , biophysics , chemistry , atpase , actin , kinetics , thermodynamics , sort , entropy (arrow of time) , entropy production , contraction (grammar) , biochemistry , physics , biology , computer science , enzyme , endocrinology , classical mechanics , information retrieval
"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.