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Tetramers formation

The fraction of unreacted groups is l p. If it is assumed that a tetramer is formed because of the reaction between 4 reactant molecules, 2 of AA and 2 of B-B, in which 3 pairs of reactive groups have reacted. The probability of a tetramer formation is, P3. [Pg.66]

The anharmonicity of the O—H stretching oscillators changes with cluster size. For the monomer, the anharmonicity constant is on the order of 90 cm 1. A coarse deuteration analysis [16, 88] suggests that it increases by more than 20% upon trimer and tetramer formation [16]. More accurate overtone analyses are possible in a rare gas matrix [88], but the matrix shift complicates a direct comparison to theory. As an example, the overtone-deduced anharmonicity of methanol monomer in a nitrogen matrix [88] is 85 cm whereas in vacuum [16] it is 92 cm The deuteration-estimated anharmonicity is 91 cm 1 for the monomer and 97 cm 1 for the dimer donor in the nitrogen matrix, whereas it is 87 cm 1 for the monomer and 89 cm 1 for the dimer donor in vacuum. Clearly, only a vacuum overtone measurement would be fully conclusive, but as the matrix study [88]... [Pg.27]

Type IV collagen subtype [ctl(IV)]2Q 2(IV) from bovine lens capsule forms a fine meshwork structure containing many branches with about 20 nm between the branching points. There are three types of supramolecular assembly of type IV collagen molecules dimer formation (with six polypeptide chains) at the C-terminal NCI domain, the association of four molecules (12 chains) in a 30 nm tetramer formation at the N-terminal 7S domain, and lateral interaction at the collagenous domain (Figure 5(a)). ° ... [Pg.484]

Originality The use of sodium sulfite as an agent to lower tetramer formation in... [Pg.215]

The current application has determined that tetramer formation can be minimized using amounts low in sodium sulfite as a reaction catalyst. [Pg.215]

Other models are also consistent with the X-ray data and the binding and kinetic data, but the three models are relatively simple. Models involving tetramer formation would not fit the above data, because it is found that the tetramer will bind up to 16 phosphates (49) ... [Pg.406]

A further possibility is that tetramer formation may have occurred in an eutectic solution. High yield of tetramer (> 10%) can be obtained by cooling dilute cyanide solutions to between - 10°C and -30°C for a few months. [Pg.97]

Fig. 2. Evolution of the spectrin superfamily. Rounded rectangles represent spectrin repeats. Shaded rectangles denote a-actinin-like repeats involved in dimerization, whereas unshaded rectangles represent repeats that were involved in duplication and/ or elongation events. The incomplete spectrin repeats involved in tetramer formation are proportionally represented depending on the number of repeat helices each protein contributes to the formation of a complete spectrin repeat. (Adapted from Dubreuil, 1991 Pascual et al., 1997.) A dystrophin/utrophin ancestor probably diverged from a-actinin at a relatively early stage and then underwent its own series of duplications and acquisitions of new motifs. Fig. 2. Evolution of the spectrin superfamily. Rounded rectangles represent spectrin repeats. Shaded rectangles denote a-actinin-like repeats involved in dimerization, whereas unshaded rectangles represent repeats that were involved in duplication and/ or elongation events. The incomplete spectrin repeats involved in tetramer formation are proportionally represented depending on the number of repeat helices each protein contributes to the formation of a complete spectrin repeat. (Adapted from Dubreuil, 1991 Pascual et al., 1997.) A dystrophin/utrophin ancestor probably diverged from a-actinin at a relatively early stage and then underwent its own series of duplications and acquisitions of new motifs.
Leukert N, Vogl T, Strupat K, Reichelt R, Sorg C, Roth J. 2006. Calcium-dependent tetramer formation of S100A8 and S100A9 is essential for biological activity. J Mol Biol 359(4) 961—972. [Pg.130]

Here we can again make a distinction between (i) oligomerization occurs by the same mechanism as polymerization and (ii) oligomerization follows a different mechanism. The first kind has been proposed by Rose (19) for the tetramer formation of oxetane up to the fourth monomer added there is no difference between polymerization and tetramer formation. For polymerization the next step is addition of a fifth monomer molecule. If the next step is reaction between the end-standing hydroxy group with the growing chain, a cyclic secondary oxonium salt is formed which leads to tetramer by a proton transfer to another ether function (see p. 109). [Pg.123]

Oligomer formation by a mechanism different from the polymerization mechanism has been proposed by Kern (7) for the tetramer formation from a number of epoxides and by Pasika (10) for styrene oxide dimer formation, although in the last case the initiation reactions are probably the same. However, in both cases degradation of polymer would be a possible alternative mechanism. [Pg.123]

Catalysis by enzymes can also be affected by crowding in a number of ways. For example, an enzyme might undergo a monomer-tetramer reaction where only the tetramer is catalytically active. If tetramer formation is favored under crowded conditions then the rate of reaction will increase. In this way, rate constants can be altered by several orders of magnitude. [Pg.114]

Polymerization from the gaseous phase (disregarding dimer to tetramer formation) is an example of a heterogeneous reaction where the active centres are present in the condensed phase and the monomer in the gaseous phase. Polymerization does not, of course, proceed in the gaseous state but on the surface of the component carrying the active centres, i. e. also in the condensed phase. These polymerizations are of industrial importance. [Pg.17]

In all the above-mentioned studies, only the tetramer has catalytic activity. The only claims for an active dimer 106,107) are not supported by satisfactory experimental evidence. Deal and co-workers 104, 108) have, on the other hand, presented extensive studies of the ATP-induced dissociation of GPD to inactive dimers and monomers at low temperatures. Furthermore, these subunits display very little unfolding, which has been taken to imply that dissociation is the major factor in the activity loss. These results were confirmed 24) with the rat skeletal muscle enzyme, which dissociates at 0° to inactive dimers in the absence of ATP. In addition, the activity transport studies of Hoagland and Teller 109) have given strong evidence that only the tetrameric form is active and that the presence of all three substrates promotes tetramer formation. It was also shown that rabbit muscle enzyme exists in a dimer-tetramer equilibrium in dilute aqueous solution at 5°, with an association constant... [Pg.25]

Tetrameric cage compounds with cubane structures have not been isolated. Tetramer formation is observed for [Mes A10]4 (34) in which the aluminum atoms remain three-coordinate and cage formation is precluded by the steric bulk of the Mes substituents. Compound (34) was prepared by reaction of [Mes AIH2]2 with [Me2SiO]3 and was not obtained by hydrolysis. [Pg.160]

The dipeptides Gly-L-His, L-Ala-L-His, and L-Ala-D-His initially form 3N complexes with palladium(II), bonding through the amino, deprotonated peptide, and imidazole nitrogens. When the pH is raised above 9.5, the pyrrole proton is ionized, resulting in a 4N tetramer formation." ... [Pg.3607]

The mechanism of tetramer formation which is reported (8, 19) involves the following steps. The reaction of a-methylstyrene with sodium produces radical-ions,... [Pg.103]

Across species the carboxyl-terminal region of apoE up to approximately residue 288 in the human sequence is highly conserved (Fig. 1). Studies to determine the carboxyl-terminal regions of apoE responsible for lipid binding and tetramer formation have been performed using three carboxyl-terminal truncations (Westerlund and Weisgraber, 1993). As shown in Fig. 19, the carboxyl terminus beyond position 191 contains three predicted a-helical regions. Two of the helices, residues... [Pg.292]

It is, of course, possible that the initial fast phase is reversible. It was concluded that removal of the C-terminal tail allows an active-site conformation to occur during turnover, in which the affinity for FMN is decreased, allowing the cofactor to dissociate from the enzyme. Thus the C-terminal tail is not essential for tetramer formation but appears to act as a conformational anchor, exerting an effect on the structure of the enzyme in regions distant from it, particularly the FMN active site. [Pg.295]

The second MAL relation for the ion trimer and tetramer formations can be written in two different forms. For the regime of a weak ion pairing (a —> 1) the trimer formation process is the dominating process and,... [Pg.55]


See other pages where Tetramers formation is mentioned: [Pg.167]    [Pg.100]    [Pg.239]    [Pg.22]    [Pg.636]    [Pg.94]    [Pg.423]    [Pg.188]    [Pg.73]    [Pg.57]    [Pg.16]    [Pg.61]    [Pg.98]    [Pg.109]    [Pg.126]    [Pg.161]    [Pg.370]    [Pg.371]    [Pg.26]    [Pg.344]    [Pg.158]    [Pg.4839]    [Pg.168]    [Pg.294]    [Pg.26]   
See also in sourсe #XX -- [ Pg.167 , Pg.167 ]




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