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Preferred repeats

CH3I should approach the enolate from the direction that simultaneously allows its optimum overlap with the electron-donor orbital on the enolate (this is the highest-occupied molecular orbital or HOMO), and minimizes its steric repulsion with the enolate. Examine the HOMO of enolate A. Is it more heavily concentrated on the same side of the six-membered ring as the bridgehead methyl group, on the opposite side, or is it equally concentrated on the two sides A map of the HOMO on the electron density surface (a HOMO map ) provides a clearer indication, as this also provides a measure of steric requirements. Identify the direction of attack that maximizes orbital overlap and minimizes steric repulsion, and predict the major product of each reaction. Do your predictions agree with the thermodynamic preferences Repeat your analysis for enolate B, leading to product B1 nd product B2. [Pg.169]

In most instances, C. difficile toxin testing of a single stool specimen effectively establishes the diagnosis. Various ELISA kits are available to detect toxin A or toxin B or both. Those that detect both toxin A and B are preferred. Repeated testing can boost sensitivity. [Pg.1123]

HPPN unit, which is produced after three deacetylation steps, is the main repeating unit in the PH A synthesized from 11-phenoxyundecanoic acid again shows that P. oleovorans prefers repeating units containing eight or nine atoms. [Pg.70]

Carry out similar runs with the solutions of monochloroacetic acid, preferably repeating the measurement of T. ... [Pg.192]

Shake 1 ml. of anhydrous methyl alcohol with 1 ml. of paraffin oil. Repeat the experiment with 1 ml. of n butyl alcohol. From your results state which is the better solvent for paraffin oil (a mixture of higher hydrocarbons) and thus explain why n-butanol and higher alcohols are incorporated in pyroxylin lacquers in preference to methyl and ethyl alcohols. [Pg.261]

Mix 50 ml. of formalin, containing about 37 per cent, of formaldehyde, with 40 ml. of concentrated ammonia solution (sp. gr. 0- 88) in a 200 ml. round-bottomed flask. Insert a two-holed cork or rubber stopper carrying a capillary tube drawn out at the lower end (as for vacuum distillation) and reaching almost to the bottom of the flask, and also a short outlet tube connected through a filter flask to a water pump. Evaporate the contents of the flask as far as possible on a water bath under reduced pressure. Add a further 40 ml. of concentrated ammonia solution and repeat the evaporation. Attach a reflux condenser to the flask, add sufficient absolute ethyl alcohol (about 100 ml.) in small portions to dissolve most of the residue, heat under reflux for a few minutes and filter the hot alcoholic extract, preferably through a hot water fuimel (all flames in the vicinity must be extinguished). When cold, filter the hexamine, wash it with a little absolute alcohol, and dry in the air. The yield is 10 g. Treat the filtrate with an equal volume of dry ether and cool in ice. A fiulher 2 g. of hexamine is obtained. [Pg.326]

Corks are badly attacked and must be renewed in each run. It is preferable to employ asbestos - sodium silicate stoppers, which can be used repeatedly. [Pg.494]

Poly(viaylidene fluoride) [24937-79-9] is the addition polymer of 1,1-difluoroethene [73-38-7], commonly known as vinylidene fluoride and abbreviated VDF or VF2. The formula of the repeat unit in the polymer is —CH2—CF2—. The preferred acronym for the polymer is PVDF, but the abbreviation PVF2 is also frequently used. The history and development of poly(vinyhdene fluoride) technology has been reviewed (1 3). [Pg.385]

The single-monomer route (eq. 5) is preferred as it proves to give more linear and para-linked repeat unit stmctures than the two-monomer route. Other sulfone-based polymers can be similarly produced from sulfonyl haUdes with aromatic hydrocarbons. The key step in these polymerisations is the formation of the carbon—sulfur bond. High polymers are achievable via this synthesis route although the resulting polymers are not always completely linear. [Pg.463]

The foremnner of the modern methods of asphalt fractionation was first described in 1916 (50) and the procedure was later modified by use of fuller s earth (attapulgite [1337-76-4]) to remove the resinous components (51). Further modifications and preferences led to the development of a variety of fractionation methods (52—58). Thus, because of the nature and varieties of fractions possible and the large number of precipitants or adsorbents, a great number of methods can be devised to determine the composition of asphalts (5,6,44,45). Fractions have also been separated by thermal diffusion (59), by dialysis (60), by electrolytic methods (61), and by repeated solvent fractionations (62,63). [Pg.367]

Acids that are solids can be purified in this way, except that distillation is replaced by repeated crystallisation (preferable from at least two different solvents such as water, alcohol or aqueous alcohol, toluene, toluene/petroleum ether or acetic acid.) Water-insoluble acids can be partially purified by dissolution in N sodium hydroxide solution and precipitation with dilute mineral acid. If the acid is required to be free from sodium ions, then it is better to dissolve the acid in hot N ammonia, heat to ca 80°, adding slightly more than an equal volume of N formic acid and allowing to cool slowly for crystallisation. Any ammonia, formic acid or ammonium formate that adhere to the acid are removed when the acid is dried in a vacuum — they are volatile. The separation and purification of naturally occurring fatty acids, based on distillation, salt solubility and low temperature crystallisation, are described by K.S.Markley (Ed.), Fatty Acids, 2nd Edn, part 3, Chap. 20, Interscience, New York, 1964. [Pg.62]

Isoxanthopterin (2-amino-4,7-dihydroxypteridine) [529-69-1] M 179.4, m>300°, pKj -0.5 (basic), pKj 7.34 (acidic), pKj 10.06 (acidic). Purified by repeated pptn from alkaline solutions by acid (preferably AcOH), filter, wash well with H2O then EtOH and dried at 100°. Purity is checked by paper chromatography [Rp 0.15 (n-BuOH, AcOH, H2O, 4 1 1) 0.33 (3% aq NH4OH). [Goto et al. Arch Biochem... [Pg.544]

Figure 1.2 shows one way of dividing a polypeptide chain, the biochemist s way. There is, however, a different way to divide the main chain into repeating units that is preferable when we want to describe the structural properties of proteins. For this purpose it is more useful to divide the polypeptide chain into peptide units that go from one Ca atom to the next Ca atom (see Figure 1.5). Each C atom, except the first and the last, thus belongs to two such units. The reason for dividing the chain in this way is that all the atoms in such a unit are fixed in a plane with the bond lengths and bond angles very nearly the same in all units in all proteins. Note that the peptide units of the main chain do not involve the different side chains (Figure 1.5). We will use both of these alternative descriptions of polypeptide chains—the biochemical and the structural—and discuss proteins in terms of the sequence of different amino acids and the sequence of planar peptide units. Figure 1.2 shows one way of dividing a polypeptide chain, the biochemist s way. There is, however, a different way to divide the main chain into repeating units that is preferable when we want to describe the structural properties of proteins. For this purpose it is more useful to divide the polypeptide chain into peptide units that go from one Ca atom to the next Ca atom (see Figure 1.5). Each C atom, except the first and the last, thus belongs to two such units. The reason for dividing the chain in this way is that all the atoms in such a unit are fixed in a plane with the bond lengths and bond angles very nearly the same in all units in all proteins. Note that the peptide units of the main chain do not involve the different side chains (Figure 1.5). We will use both of these alternative descriptions of polypeptide chains—the biochemical and the structural—and discuss proteins in terms of the sequence of different amino acids and the sequence of planar peptide units.

See other pages where Preferred repeats is mentioned: [Pg.1114]    [Pg.120]    [Pg.2516]    [Pg.1114]    [Pg.1114]    [Pg.69]    [Pg.593]    [Pg.42]    [Pg.1114]    [Pg.120]    [Pg.2516]    [Pg.1114]    [Pg.1114]    [Pg.69]    [Pg.593]    [Pg.42]    [Pg.112]    [Pg.16]    [Pg.35]    [Pg.203]    [Pg.232]    [Pg.444]    [Pg.455]    [Pg.154]    [Pg.164]    [Pg.311]    [Pg.901]    [Pg.1037]    [Pg.1040]    [Pg.1041]    [Pg.235]    [Pg.442]    [Pg.312]    [Pg.371]    [Pg.401]    [Pg.34]    [Pg.459]    [Pg.33]    [Pg.49]    [Pg.286]    [Pg.56]    [Pg.361]    [Pg.370]   


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