Photoaffinity labeling of scallop myosin with 2-[(4-azido-2-nitrophenyl)amino]ethyl diphosphate: identification of an active site arginine analogous to tryptophan-130 in skeletal muscle myosin

1992 ◽  
Vol 3 (4) ◽  
pp. 328-336 ◽  
Author(s):  
Bruce A. Kerwin ◽  
Ralph G. Yount
Keyword(s):  
Skeletal Muscle ◽  
Active Site ◽  
Photoaffinity Labeling ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

A model for the active site of skeletal muscle myosin

1979 ◽  
Vol 76 (3) ◽  
pp. 351-357 ◽  
Author(s):  
F. Ramirez ◽  
K.K. Shukla ◽  
H.M. Levy
Keyword(s):  
Skeletal Muscle ◽  
Active Site ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

Characterization of the active site of platelet myosin in comparison to smooth and skeletal muscle myosin

1976 ◽  
Vol 175 (1) ◽  
pp. 249-255 ◽  
Author(s):  
Isaac Cohen ◽  
Elizabeth Kaminski ◽  
Raphael Lamed ◽  
Avraham Oplatka ◽  
Andras Mühlrad
Keyword(s):  
Skeletal Muscle ◽  
Active Site ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

scholarly journals Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase.

1985 ◽  
Vol 260 (20) ◽  
pp. 11275-11285 ◽  
Author(s):  
A M Edelman ◽  
K Takio ◽  
D K Blumenthal ◽  
R S Hansen ◽  
K A Walsh ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Skeletal Muscle Myosin ◽  
Calmodulin Binding ◽  
Catalytic Domains ◽  
Muscle Myosin

scholarly journals Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay.

1993 ◽  
Vol 268 (27) ◽  
pp. 20414-20418
Author(s):  
S Lowey ◽  
G.S. Waller ◽  
K.M. Trybus
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Motility Assay ◽  
In Vitro Motility Assay ◽  
Skeletal Muscle Myosin ◽  
In Vitro Motility ◽  
Muscle Myosin

Cloning and in Situ Hybridization of Type 2A and 2B Rat Skeletal Muscle Myosin Tail Region: Implications for Filament Assembly

1993 ◽  
Vol 197 (3) ◽  
pp. 1312-1318 ◽  
Author(s):  
R.L. Lieber ◽  
S.C. Bodine ◽  
T.J. Burkholder ◽  
D.J. Pierotti ◽  
A.F. Ryan
Keyword(s):  
Skeletal Muscle ◽  
In Situ Hybridization ◽  
Rat Skeletal Muscle ◽  
Tail Region ◽  
Skeletal Muscle Myosin ◽  
Filament Assembly ◽  
Muscle Myosin

scholarly journals Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation.

1975 ◽  
Vol 67 (1) ◽  
pp. 93-104 ◽  
Author(s):  
T D Pollard
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Structural Features ◽  
Length Frequency ◽  
Single Population ◽  
Skeletal Muscle Myosin ◽  
Distinctive Features ◽  
Myosin Filaments ◽  
The Mean ◽  
Muscle Myosin

Electron micrographs of negatively stained synthetic myosin filaments reveal that surface projections, believed to be the heads of the constituent myosin molecules, can exist in two configurations. Some filaments have the projections disposed close to the filament backbone. Other filaments have all of their projections widely spread, tethered to the backbone by slender threads. Filaments formed from the myosins of skeletal muscle, smooth muscle, and platelets each have distinctive features, particularly their lengths. Soluble mixtures of skeletal muscle myosin with either smooth muscle myosin or platelet myosin were dialyzed against 0.1 M KC1 at pH 7 to determine whether the simultaneous presence of two types of myosin would influence the properties of the filaments formed. In every case, a single population of filaments formed from the mixtures. The resulting filaments are thought to be copolymers of the two types of myosin, for several reasons: (a) their length-frequency distribution is unimodal and differs from that predicted for a simple mixture of two types of myosin filaments; (b) their mean length is intermediate between the mean lengths of the filaments formed separately from the two myosins in the mixture; (c) each of the filaments has structural features characteristic of both of the myosins in the mixture; and (d) their size and shape are determined by the proportion of the two myosins in the mixture.

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