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Y shape molecule

Antibodies are large Y-shaped molecules having a molecular mass of 000 ia which the domains forming the tips of the arm biad to the... [Pg.248]

Figure 2 shows the most abundant class of antibodies found in blood serum and lymph - immunoglobulin G (IgG). IgG of molecular mass about 156 000, is most frequently used as a receptor in immunosensors. According to X-ray data6 8, IgG is a Y-shaped molecule consisting of two identical antigen binding Fab arms of dimensions 6.5 nm by 3.5 nm and an inactive Fc shank of dimensions 5 nm by 3.5 nm. [Pg.388]

The basic structure of an immunoglobulin molecule, such as the major serum antibody IgG, consists of four polypeptide chains two identical light chains (molecular weight around 25 000 daltons) and two identical heavy chains (with a molecular weight around 50 000 daltons), cross-linked by disulfide bonds to form Y-shaped molecules with two flexible arms (Fig. 11.2). The binding sites are located on the arms and vary from one molecule to another (variable region) [22b]. [Pg.304]

Branching can also lead to the formation of densely connected networks. For example, if we start with a Y-shaped molecule, where each arm of the Y has a reactive group that is capable of reacting with and connecting to any other group on another Y,... [Pg.26]

The equilibrium geometries, one-, two-, and three-photon absorption properties, and the transition nature of a series of Y-shaped molecules which possess an imidazole-thiazole core have been studied theoretically using the parametrization model 3 and Zerner s intermediate neglect of differential overlap (ZINDO) methods <2006JCP024704>. [Pg.641]

Fig. 3.2. Model of the cytochrome oxidase monomer. The structural model of the membrane-bound cytochrome oxidase monomer that has emerged from image reconstruction studies of two-dimensional crystals [102-106] is an asymmetric Y -shaped molecule (see also Ref. 99). A considerable part protrudes on the cytoplasmic side of the membrane, but only little on the M side. In the membrane there are two separated domains. Chemical labelling and cross-Unking studies (see Refs. 85, 92, 95, 96, 99 for reviews) have given at least a rough topography of the individual subunits. The protruding C-domain is made up mainly of subunits I, II, III and V, while the aqueous M-domain is largely due to subunit IV. The two membranous domains are formed by subunits I and III, but also subunits II, IV, Villa and Vlllb (Table 3.3) probably contribute with 2, 1, 1 and 1 transmembranous polypeptide segments, respectively. Fig. 3.2. Model of the cytochrome oxidase monomer. The structural model of the membrane-bound cytochrome oxidase monomer that has emerged from image reconstruction studies of two-dimensional crystals [102-106] is an asymmetric Y -shaped molecule (see also Ref. 99). A considerable part protrudes on the cytoplasmic side of the membrane, but only little on the M side. In the membrane there are two separated domains. Chemical labelling and cross-Unking studies (see Refs. 85, 92, 95, 96, 99 for reviews) have given at least a rough topography of the individual subunits. The protruding C-domain is made up mainly of subunits I, II, III and V, while the aqueous M-domain is largely due to subunit IV. The two membranous domains are formed by subunits I and III, but also subunits II, IV, Villa and Vlllb (Table 3.3) probably contribute with 2, 1, 1 and 1 transmembranous polypeptide segments, respectively.
One consequence of the intramolecular incorporation of macromer is that each site incorporates only macromer that it produced itself. That is, cross-insertion by one site of macromer produced on another site should happen rarely or not at all. Evidence from experiments with metallocene catalysts [533] in slurry polymerizations failed to produce any evidence of "cross-insertion" between sites. This finding means that LCB can be concentrated within any region of the MW distribution. Another expected result is that sites producing long backbone chains should also produce long branches, and short backbones should contain short branches, so called "Y-shaped" molecules. [Pg.294]

Antibodies, or immunoglobulins, are globular proteins with molecular weights of 150 to 200 kdal. They are made up of four subunits, two "heavy" and two "light" chains, which together form a "Y"-shaped molecule. The stem of the antibody is referred to as the "constant" or F region, while the two branches containing the... [Pg.209]

The general immunoglobulin structure is a 4-chain Y -shaped molecule of two heavy-chain and two light-chain polypeptides joined together by disulfide bridges... [Pg.852]

All antibodies share a common scaffold (Figure 1) [7]. Two heavy and two light chains combine to form a homodimeric, Y-shaped molecule of Mr 160,(XX). The antigen-binding sites are located in the N-terminal variable... [Pg.341]

Figure 9.2 (a) Example of structuring of water (blue, or light gray Y shaped molecules) and acetone (purple or darker gray) molecules in the shell around a PCL chain (white spheres) constituted by 30 monomers in a equimolar water-acetone mixture instantaneous realization obtained by molecular dynamics simulation, (b) Snapshots of the molecular dynamics simulation of the same PCL chain, visible in white at the center of the simulation box, in an equimolar acetone-water mixture, showing how the polymer shape modifies and the acetone clustering phenomenon of the liquid around the polymer the water is represented in yellow, while acetone is not shown for clarity (courtesy of Nicodemo Di Pasquale). [Pg.236]


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See also in sourсe #XX -- [ Pg.259 ]




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