Myosin dynamics on the millisecond time scale

Thomas P. Burghardt, Jimmy Yan Hu, Katalin Ajtai

Research output: Contribution to journalArticlepeer-review

Abstract

Myosin is a motor protein associating with actin and ATP. It translates along actin filaments against a force by transduction of free energy liberated with ATP hydrolysis. Various myosin crystal structures define time points during ATPase showing the protein undergoes large conformation change during transduction over a cycle with ∼ 10 ms periodicity. The protein conformation trajectory between two intermediates in the cycle is surmised by non-equilibrium Monte Carlo simulation utilizing free-energy minimization. The trajectory shows myosin transduction of free energy to mechanical work giving evidence for: (i) a causal relationship between product release and work production in the native isoform that is correctly disrupted in a chemically modified protein, (ii) the molecular basis of ATP-sensitive tryptophan fluorescence enhancement and acrylamide quenching, (iii) an actin-binding site peptide containing the free-energy barrier to ATPase product release defining the rate limiting step and, (iv) a scenario for actin-activation of myosin ATPase.

Original languageEnglish (US)
Pages (from-to)15-28
Number of pages14
JournalBiophysical Chemistry
Volume131
Issue number1-3
DOIs
StatePublished - Dec 2007

Keywords

  • Contractility
  • Fluorescence quenching mechanism
  • Free energy minimization
  • Granger causality
  • Motor protein structure-function
  • Non-equilibrium Monte Carlo simulation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry

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