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Torpedo lines

Torpedo lines shall be bright (uncoated) or drawn-galvanized, and shall be right, regular lay. The lay of the finished rope shall not exceed eight times the nominal diameter. [Pg.578]

Torpedo lines shall be made of five strands of five wires each, or five strands of seven wires each. The strands of the 5x5 construction shall have one center wire and four outer wires of one diameter, fabricated in one operation. The five strands shall be laid around one fiber or cotton core (see Figure 4-66). The strands of the 5x7 construction shall have one center wire and six outer wires of one diameter, fabricated in one operation. The strands shall be laid around one fiber or cotton core (see Figure 4-67). [Pg.578]

The nominal strength of torpedo lines shall be as specified in Tables 4-26 and 4-27. When testing finished ropes to their breaking strength, suitable sockets... [Pg.578]

The diameter of the ropes shall be not less than the specified diameter. Torpedo-line lengths shall vary in 500-ft (152.4 m) multiples. [Pg.580]

Fig. 11.2. Schematic representation of the primary structure of secreted AChE B of N. brasiliensis in comparison with that of Torpedo californica, for which the three-dimensional structure has been resolved. The residues in the catalytic triad (Ser-His-Glu) are depicted with an asterisk, and the position of cysteine residues and the predicted intramolecular disulphide bonding pattern common to cholinesterases is indicated. An insertion of 17 amino acids relative to the Torpedo sequence, which would predict a novel loop at the molecular surface, is marked with a black box. The 14 aromatic residues lining the active-site gorge of the Torpedo enzyme are illustrated. Identical residues in the nematode enzyme are indicated in plain text, conservative substitutions are boxed, and non-conservative substitutions are circled. The amino acid sequence of AChE C is 90% identical to AChE B, and differs only in the features illustrated in that Thr-70 is substituted by Ser. Fig. 11.2. Schematic representation of the primary structure of secreted AChE B of N. brasiliensis in comparison with that of Torpedo californica, for which the three-dimensional structure has been resolved. The residues in the catalytic triad (Ser-His-Glu) are depicted with an asterisk, and the position of cysteine residues and the predicted intramolecular disulphide bonding pattern common to cholinesterases is indicated. An insertion of 17 amino acids relative to the Torpedo sequence, which would predict a novel loop at the molecular surface, is marked with a black box. The 14 aromatic residues lining the active-site gorge of the Torpedo enzyme are illustrated. Identical residues in the nematode enzyme are indicated in plain text, conservative substitutions are boxed, and non-conservative substitutions are circled. The amino acid sequence of AChE C is 90% identical to AChE B, and differs only in the features illustrated in that Thr-70 is substituted by Ser.
The initial solution of the crystal structure of the Torpedo enzyme [28], followed by the mammalian AChE structure [29], revealed that the active center serine lies at the base of a rather narrow gorge that is lined heavily with aromatic residues (Fig. 11-6). The enzyme carries a net negative charge, and an electrostatic dipole is oriented on the enzyme to facilitate diffusional entry of cationic ligands. Crystal structures of several inhibitors in a complex with AChE also have been elucidated [25]. [Pg.195]

Concentration-effect curve of an antagonist ( , d-tubocurarine + agonist) and agonist alone ( , suberyldicho-line) at Torpedo nAChR expressed in oocytes (unpublished observations)... [Pg.337]

As to Japanese ammunition itself, one can point out the great variety of improvised devices, such as Mines Depth Charges made from wooden boxes, burlap bags with rubber lining, oil drums Grenades made of pottery, glass gas pipes Booby Traps made of tin cans and Bangalore Torpedoes made of bamboo tubes... [Pg.452]

Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., Silman, I. (1991). Atomic structme of acetylcholinesterase from Torpedo califomica a prototypic acetylcho-line-hinding protein. Science 253 872-9. [Pg.1064]


See other pages where Torpedo lines is mentioned: [Pg.544]    [Pg.578]    [Pg.579]    [Pg.579]    [Pg.579]    [Pg.579]    [Pg.544]    [Pg.578]    [Pg.579]    [Pg.579]    [Pg.579]    [Pg.579]    [Pg.274]    [Pg.163]    [Pg.114]    [Pg.852]    [Pg.203]    [Pg.110]    [Pg.64]    [Pg.116]    [Pg.185]    [Pg.220]    [Pg.224]    [Pg.225]    [Pg.452]    [Pg.175]    [Pg.50]    [Pg.323]    [Pg.469]    [Pg.45]    [Pg.56]    [Pg.78]    [Pg.200]    [Pg.661]    [Pg.274]    [Pg.878]    [Pg.17]    [Pg.56]    [Pg.1695]    [Pg.3]    [Pg.183]    [Pg.291]    [Pg.291]    [Pg.217]    [Pg.852]    [Pg.469]   
See also in sourсe #XX -- [ Pg.578 , Pg.579 ]




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