Decrease in light diffraction intensity of contracting muscle fibres

1988 ◽  
Vol 15 (6) ◽  
Author(s):  
A.F. Leung ◽  
M.K. Cheung
Keyword(s):  
Light Diffraction ◽  
Muscle Fibres ◽  
Diffraction Intensity ◽  
Contracting Muscle

Orientation of spin labels attached to cross-bridges in contracting muscle fibres

Nature ◽  
1982 ◽  
Vol 300 (5894) ◽  
pp. 776-778 ◽  
Author(s):  
Roger Cooke ◽  
Mark S. Crowder ◽  
David D. Thomas
Keyword(s):  
Spin Labels ◽  
Muscle Fibres ◽  
Contracting Muscle ◽  
Cross Bridges

Light diffraction studies of active muscle fibres as a function of sarcomere length

1981 ◽  
Vol 2 (2) ◽  
pp. 215-224 ◽  
Author(s):  
Toshiharu Oba ◽  
Ronald J. Baskin ◽  
Richard L. Lieber
Keyword(s):  
Sarcomere Length ◽  
Light Diffraction ◽  
Muscle Fibres ◽  
Active Muscle

The actomyosin ATPase: a two-state system

1992 ◽  
Vol 336 (1276) ◽  
pp. 63-71 ◽  
Keyword(s):  
Equilibrium Constants ◽  
Muscle Fibres ◽  
Close Coupling ◽  
Contracting Muscle ◽  
Myosin Subfragment ◽  
Association Reaction ◽  
Myosin Subfragment 1 ◽  
Series Of Experiments ◽  
Contraction Cycle ◽  
Key Events

Studies of the interaction between actin and myosin subfragment 1 (S1) in solution have shown that the association reaction takes place in at least two steps. Initially the association is relatively weak to form a complex called the A state which can then isomerize to the R state. The rate and equilibrium constants for the isomerization have been measured and are shown to depend upon the nucleotide bound to the SI ATPase site; with ATP bound the A state is preferred but as ATP is hydrolysed and the products are sequentially released then the complex gradually shifts to the A state. An extensive series of experiments have characterized the A-to-R isomerization both in solution and in contracting muscle fibres and have shown it to be closely associated with the key events in the ATP-driven contraction cycle: the conformational change from the A to the R state can be monitored by fluorescent probes on either actin or the nucleotide; the isomerization can be perturbed by increases in hydrostatic pressure; the actin-induced acceleration of the rate of product release from myosin is coupled to the A-to-R isomerization; tropomyosin may control actin and myosin interaction by controlling the ismoerization step and finally pressure perturbations of contracting muscle fibres shows there to be a close coupling between the isomerization of acto.S1 and the force generating event of muscle contraction.

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