Bony fish muscles diffraction patterns from

A typical low-angle diffraction pattern from relaxed bony fish muscle is shown in Fig. 4B. Much of the intensity that is seen comes from the organization of the myosin heads on the myosin filaments in the resting state (probably mainly MADP.Pi). We know that the myosin heads lie approximately on three co-axial helices of subunit translation 143 A and repeat 429 A. This is most easily represented by the radial net shown in Fig. 16B-D. The radial net in D is like an opened-out surface view of the filament in B. Here the helical tracks become straight lines, and the black blobs represent the origins on the myosin filament surface of the pairs of myosin heads in each myosin molecule. From early studies it is known that the three crowns within the 429 A repeat are not exactly the same and that there is a perturbation. [Pg.55]

Fig. 12. (A) The left half of a low-angle diffraction pattern from bony fish muscle...

$Fig. 12. (A) The left half of a low-angle diffraction pattern from bony fish muscle...$

Fig. 13. Illustrations of the possible arrangement of C-protein (MyBP-C) on the myosin filament backbone in projection down the axis (A) and in axial view (B). Of particular importance here is the possibility that the N-terminal half of C-protein extends out and binds to actin in relaxed muscle. (C) Simulation of the possible interactions of C-protein with binding sites on actin generated using the program MusLABEL (Squire and Knupp, 2004). (D) Left left half of the low-angle X-ray diffraction pattern from bony fish muscle (as in Fig. 11C), showing (right) the possible positions where the C-protein array in (D) might contribute. (From Squire elal, 2003d.)...

$Fig. 13. Illustrations of the possible arrangement of C-protein (MyBP-C) on the myosin filament backbone in projection down the axis (A) and in axial view (B). Of particular importance here is the possibility that the N-terminal half of C-protein extends out and binds to actin in relaxed muscle. (C) Simulation of the possible interactions of C-protein with binding sites on actin generated using the program MusLABEL (Squire and Knupp, 2004). (D) Left left half of the low-angle X-ray diffraction pattern from bony fish muscle (as in Fig. 11C), showing (right) the possible positions where the C-protein array in (D) might contribute. (From Squire elal, 2003d.)...$

Fig. 15. Intensity profiles along the equator of the bony fish muscle low angle X-ray diffraction pattern from muscles at rest (A), fully active (B), and in rigor (C). The indexing in (A) is based on the hexagonal A-band lattice, and the arrows indicate peaks that come from the Z-band. (C) to (F) are computed electron density maps based on the amplitudes of the A-band peaks in (A) to (A), respectively. The simple lattice unit cell is outlined in (D). (From Harford and Squire, 1997.)...

$Fig. 15. Intensity profiles along the equator of the bony fish muscle low angle X-ray diffraction pattern from muscles at rest (A), fully active (B), and in rigor (C). The indexing in (A) is based on the hexagonal A-band lattice, and the arrows indicate peaks that come from the Z-band. (C) to (F) are computed electron density maps based on the amplitudes of the A-band peaks in (A) to (A), respectively. The simple lattice unit cell is outlined in (D). (From Harford and Squire, 1997.)...$

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