Filaments, thin

The coin-tap test is a widely used teclinique on thin filament winded beams for detection of disbonded and delaminated areas. However, since the sensitivity of this teclinique depends not only on the operator but also on the thickness of the inspected component, the coin-tap testing technique is most sensitive to defects positioned near the surface of the laminate. Therefore, it was decided to constructed a new scaimer for automated ultrasonic inspection of filament winded beams. A complete test rig illustrated in figure 6 was constructed in order to reduce the scanning time. While the beam rotates the probe is moved from one end to the other of the beam. When the scarming is complete it is saved on diskette and can then be evaluated on a PC. The scanner is controlled by the P-scan system, which enables the results to be presented in three dimensions (Top, Side and End view). 

Proteins can be broadly classified into fibrous and globular. Many fibrous proteins serve a stmctural role (11). CC-Keratin has been described. Fibroin, the primary protein in silk, has -sheets packed one on top of another. CoUagen, found in connective tissue, has a triple-hehcal stmcture. Other fibrous proteins have a motile function. Skeletal muscle fibers are made up of thick filaments consisting of the protein myosin, and thin filaments consisting of actin, troponin, and tropomyosin. Muscle contraction is achieved when these filaments sHde past each other. Microtubules and flagellin are proteins responsible for the motion of ciUa and bacterial dageUa. 

Within each sarcomere the relative sliding of thick and thin filaments is brought about by "cross-bridges," parts of the myosin molecules that stick out from the myosin filaments and interact cyclically with the thin actin filaments, transporting them hy a kind of rowing action. During this process, the hydrolysis of ATP to ADP and phosphate couples the conformational... 

Regarding a historical perspective on carbon nanotubes, very small diameter (less than 10 nm) carbon filaments were observed in the 1970 s through synthesis of vapor grown carbon fibers prepared by the decomposition of benzene at 1100°C in the presence of Fe catalyst particles of 10 nm diameter [11, 12]. However, no detailed systematic studies of such very thin filaments were reported in these early years, and it was not until lijima s observation of carbon nanotubes by high resolution transmission electron microscopy (HRTEM) that the carbon nanotube field was seriously launched. A direct stimulus to the systematic study of carbon filaments of very small diameters came from the discovery of fullerenes by Kroto, Smalley, and coworkers [1], The realization that the terminations of the carbon nanotubes were fullerene-like caps or hemispheres explained why the smallest diameter carbon nanotube observed would be the same as the diameter of the Ceo molecule, though theoretical predictions suggest that nanotubes arc more stable than fullerenes of the same radius [13]. The lijima observation heralded the entry of many scientists into the field of carbon nanotubes, stimulated especially by the un-... 

FIGURE 17.12 Electron micrograph of a skeletal muscle myofibril (in longitndinal section). The length of one sarcomere is indicated, as are the A and I bands, the H zone, the M disk, and the Z lines. Cross-sections from the H zone show a hexagonal array of thick filaments, whereas the I band cross-section shows a hexagonal array of thin filaments. (Photo courtesy of Hugh Huxley, Brandeis University)... 

FIGURE 17.21 A drawing of the arrangement of the elastic protein titin in the skeletal mnscle sarcomere. Titin filaments originate at the periphery of the M band and extend along the myosin filaments to the Z lines. These titin filaments produce the passive tension existing in myofibrils that have been stretched so that the thick and thin filaments no longer overlap and cannot interact. (Adapted from Ohtsuki, ., Maruyama, K, and Ebashi,. S ., 1986. Advances ia Protein Chemisti y 38 1—67.)... 

Szent-Gyorgyi further showed that the viscosity of an actomyosin solution was lowered by the addition of ATP, indicating that ATP decreases myosin s affinity for actin. Kinetic studies demonstrated that myosin ATPase activity was increased substantially by actin. (For this reason, Szent-Gyorgyi gave the name actin to the thin filament protein.) The ATPase turnover number of pure myosin is 0.05/sec. In the presence of actin, however, the turnover number increases to about 10/sec, a number more like that of intact muscle fibers. 

Actin thin filaments consist of actin, tropomyosin, and the troponins in a 7 1 1 ratio (Figure 17.15). Each tropomyosin molecule spans seven actin molecules, lying along the thin filament groove, between pairs of actin monomers. 

FIGURE 17.29 A drawing of the thick and thin filaments of skeletal mnscle in cross-section showing the changes that are postulated to occur when Ca binds to troponin C. 

The principal molecular constituent of thin filaments is actin. Actin has been highly conserved during the course of evolution and is present in all eukaryotes, including single-celled organisms such as yeasts. Actin was first extracted and purified from skeletal muscle, where it forms the thin filaments of sarcomeres. It also is the main contractile protein of smooth muscle. Refined techniques for the detection of small amounts of actin (e.g., immunofluorescence microscopy, gel electrophoresis, and EM cytochemistry) subsequently confirmed the presence of actin in a great variety of nonmuscle cells. Muscle and nonmuscle actins are encoded by different genes and are isoforms. 

Figure 1. Muscle development. A skeletal muscle fiber is formed by the fusion of many single cells (myoblasts) into a multinucleated myotube. Myotubes then develop into the muscle fiber (see text). Sarcomeres form in longitudinal structures called myofibrils. The repeating structure of the sarcomere contains interdigitating thick and thin filaments.

The A-bands contain both the myosin-containing thick filaments and the actin-containing thin filaments. In the A-bands, each thick filament is surrounded by six thin filaments (Figure 3) such that the two types of filament overlap, although the... 

Figure 3. Structure of a muscle sarcomere. In a polarizing microscope muscle appears to have dark (A) and light (I) bands. The l-band region only contains thin filaments. The A-band region contains both thick and thin filaments. One sarcomere is the distance between two Z-lines. In cross section, the hexagonal packing of the thick and thin filaments can be seen.

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