Parking problem and negative cooperativity of binding of myosin subfragment 1 to F-actin

Yana K. Reshetnyak, Cynthia N. Prudence, James Segala, Vladislav S. Markin, Oleg A. Andreev

Research output: Contribution to journalArticlepeer-review


Previously we provided evidence that myosin subfragment 1 (S1) can bind either one (state 1) or two actin monomers (state 2) in solution and in muscle fiber. Here we present results of the kinetics study of binding of S1 to F-actin labeled with fluorescent dye pyrene. A transition from state 1 to state 2 depends on probability that the second actin is free, which is high when molar ratio of S1/actin (R) is less than 0.5, and it decreases dramatically when R>2.0 due to the parking problem. The kinetics data obtained at different molar ratios were well fitted by two binding states model. The sequential binding of myosin head initially with one actin monomer and then with the second actin monomer in F-actin can play a key role in force generation by actin-myosin and their directed movement.

Original languageEnglish (US)
Pages (from-to)746-749
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Sep 7 2012


  • Actin
  • Binding kinetics
  • Muscle contraction
  • Myosin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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