Thiol-Specific Cross-Linkers of Variable Length Reveal a Similar Separation of SH1 and SH2 in Myosin Subfragment 1 in the Presence and Absence of MgADP†

Biochemistry ◽  
1999 ◽  
Vol 38 (32) ◽  
pp. 10307-10317 ◽  
Author(s):  
Werner Kliche ◽  
Jens Pfannstiel ◽  
Markus Tiepold ◽  
Stanka Stoeva ◽  
Heinz Faulstich
Keyword(s):  
Variable Length ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Presence And Absence

Binding of gizzard smooth muscle myosin subfragment-1 to actin in the presence and absence of adenosine 5'-triphosphate

Biochemistry ◽  
1983 ◽  
Vol 22 (3) ◽  
pp. 530-535 ◽  
Author(s):  
Lois E. Greene ◽  
James R. Sellers ◽  
Evan Eisenberg ◽  
Robert S. Adelstein
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Presence And Absence ◽  
Muscle Myosin

Structure of Myosin Subfragment-1 from Electron Microscopy and Crystallography

1988 ◽  
Vol 46 ◽  
pp. 156-157
Author(s):  
Donald A. Winkelmann
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Actin Filaments ◽  
Light Chains ◽  
Myosin Filament ◽  
Primary Role ◽  
Heavy Chains ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Globular Head

The primary role of the interaction of actin and myosin is the generation of force and motion as a direct consequence of the cyclic interaction of myosin crossbridges with actin filaments. Myosin is composed of six polypeptides: two heavy chains of molecular weight 220,000 daltons and two pairs of light chains of molecular weight 17,000-23,000. The C-terminal portions of the myosin heavy chains associate to form an α-helical coiled-coil rod which is responsible for myosin filament formation. The N-terminal portion of each heavy chain associates with two different light chains to form a globular head that binds actin and hydrolyses ATP. Myosin can be fragmented by limited proteolysis into several structural and functional domains. It has recently been demonstrated using an in vitro movement assay that the globular head domain, subfragment-1, is sufficient to cause sliding movement of actin filaments.The discovery of conditions for crystallization of the myosin subfragment-1 (S1) has led to a systematic analysis of S1 structure by x-ray crystallography and electron microscopy. Image analysis of electron micrographs of thin sections of small S1 crystals has been used to determine the structure of S1 in the crystal lattice.

scholarly journals Studies of Ligand-induced Conformational Perturbations in Myosin Subfragment 1

1989 ◽  
Vol 264 (18) ◽  
pp. 10810-10819
Author(s):  
K N Rajasekharan ◽  
M Mayadevi ◽  
M Burke
Keyword(s):  
Myosin Subfragment ◽  
Myosin Subfragment 1
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