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Rayment, Ivan

FIGURE 17.23 The mechanism of skeletal muscle contraction. The free energy of ATP hydrolysis drives a conformational change in the myosin head, resulting in net movement of the myosin heads along the actin filament. Inset) A ribbon and space-filling representation of the actin—myosin interaction. (SI myosin image courtesy of Ivan Rayment and Hazel M. Holden, University of Wiseonsin, Madison.)... [Pg.553]

Figure 7-10 (A) Model of the F-actin helix composed of eight monomeric subunits. The model was constructed from the known structure of the actin monomer with bound ADP using X-ray data from oriented gels of fibrous actin to deduce the helical arrangement of subunits. The main interactions appear to be along the two-start helix. See also Holmes ef a/.62 (B) Ribbon drawing of an actin monomer with the four domains labeled. Courtesy of Ivan Rayment. Figure 7-10 (A) Model of the F-actin helix composed of eight monomeric subunits. The model was constructed from the known structure of the actin monomer with bound ADP using X-ray data from oriented gels of fibrous actin to deduce the helical arrangement of subunits. The main interactions appear to be along the two-start helix. See also Holmes ef a/.62 (B) Ribbon drawing of an actin monomer with the four domains labeled. Courtesy of Ivan Rayment.
Figure 19-17 Ribbon drawing of human kinesin with bound Mg ADP. From Gulick rf a/.174 Courtesy of Ivan Rayment and Andy Gulick. Figure 19-17 Ribbon drawing of human kinesin with bound Mg ADP. From Gulick rf a/.174 Courtesy of Ivan Rayment and Andy Gulick.
B) Ribbon drawing of an actin monomer with the four domains labeled. Courtesy of Ivan Rayment. [Pg.338]

Illinois University Jim Olson, Iowa State University Ivan Rayment, University of Wisconsin John Robyt, Iowa State University Kevin Sarge, University of Kentucky Andrzej Stasiak, Universite de Lausanne Laurey Steinke, University of Nebraska Medical Center Marvin Stromer, Iowa State University Robert... [Pg.21]


See other pages where Rayment, Ivan is mentioned: [Pg.294]    [Pg.544]    [Pg.182]    [Pg.183]    [Pg.183]    [Pg.182]    [Pg.183]    [Pg.183]    [Pg.18]    [Pg.420]    [Pg.193]    [Pg.172]    [Pg.151]   
See also in sourсe #XX -- [ Pg.29 , Pg.294 , Pg.342 ]




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