Literature DB >> 2941036

The structure of myosin and its role in energy transduction in muscle.

J W Shriver.   

Abstract

The present understanding of the relationship between the structure of the myosin ATPase and its role in force production for muscle contraction is reviewed. Emphasis is placed on structural transitions in myosin that occur during ATP hydrolysis which may be correlated with force production. Although detailed structural information is presently lacking, numerous spectroscopic and kinetic experiments have indicated that myosin exists in two structural states for each chemical intermediate in the hydrolysis of ATP. Models are discussed which view a transition between these two states as the energy transduction "event" (i.e., force production).

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Year:  1986        PMID: 2941036     DOI: 10.1139/o86-038

Source DB:  PubMed          Journal:  Biochem Cell Biol        ISSN: 0829-8211            Impact factor:   3.626


  5 in total

1.  Actin and temperature effects on the cross-linking of the SH1-SH2 helix in myosin subfragment 1.

Authors:  L K Nitao; E Reisler
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

Review 2.  The dynamics of actin and myosin association and the crossbridge model of muscle contraction.

Authors:  M A Geeves
Journal:  Biochem J       Date:  1991-02-15       Impact factor: 3.857

3.  Protein fluorescence changes associated with ATP and adenosine 5'-[gamma-thio]triphosphate binding to skeletal muscle myosin subfragment 1 and actomyosin subfragment 1.

Authors:  N C Millar; M A Geeves
Journal:  Biochem J       Date:  1988-02-01       Impact factor: 3.857

4.  A transient kinetic study of enthalpy changes during the reaction of myosin subfragment 1 with ATP.

Authors:  N C Millar; J V Howarth; H Gutfreund
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857

Review 5.  Functional sequences of the myosin head.

Authors:  D Mornet; A Bonet; E Audemard; J Bonicel
Journal:  J Muscle Res Cell Motil       Date:  1989-02       Impact factor: 2.698

  5 in total

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