Myosin Dynamics on the Millisecond Time Scale

Overview

Journal Biophys Chem

Specialty Biochemistry

Date 2007 Oct 5

PMID 17913331

Citations 4

Authors

Thomas P Burghardt

Jimmy Yan Hu

Katalin Ajtai

Affiliations

Soon will be listed here.

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 approximately 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.

Citing Articles

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Myosin individualized: single nucleotide polymorphisms in energy transduction.

Burghardt T, Neff K, Wieben E, Ajtai K BMC Genomics. 2010; 11:172.

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The myosin C-loop is an allosteric actin contact sensor in actomyosin.

Ajtai K, Halstead M, Nyitrai M, Penheiter A, Zheng Y, Burghardt T Biochemistry. 2009; 48(23):5263-75.

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Energetics of subdomain movements and fluorescence probe solvation environment change in ATP-bound myosin.

Harris M, Woo H Eur Biophys J. 2008; 38(1):1-12.

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