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Molecule-substrate combination

The heat of adsorption is measured more frequently by desorption, by breaking the adsorbate-surface bond. For each molecule-substrate combination, there is an optimum temperature at which the adsorbed molecules are removed at a maximum rate. By rapidly heating the surface (at rates of a few degrees per second) to this optimum temperature, the adsorbed molecules are removed at a maximum rate before their surface concentration is depleted. Working from this optimum tempera-... [Pg.301]

Both experimental and theoretical research aim to elucidate why for some molecule-substrate combinations the desired supramolecular structure formation develops and for others it does not. With the gathered knowledge, the tailoring of the molecular components to promote molecular recognition for noncovalent bond formation together with the choice of the right support is to be propelled. [Pg.699]

The LC/TOF instmment was designed specifically for use with the effluent flowing from LC columns, but it can be used also with static solutions. The initial problem with either of these inlets revolves around how to remove the solvent without affecting the substrate (solute) dissolved in it. Without this step, upon ionization, the large excess of ionized solvent molecules would make it difficult if not impossible to observe ions due only to the substrate. Combined inlet/ionization systems are ideal for this purpose. For example, dynamic fast-atom bombardment (FAB), plas-maspray, thermospray, atmospheric-pressure chemical ionization (APCI), and electrospray (ES)... [Pg.163]

Enzyme activity refers to the rate at which a particular enzyme catalyzes the conversion of a particular substrate (or substrates) to one or more products under a given set of conditions. Usually, activity refers to the contribution of many enzyme molecules (often expressed simply as activity per mg of protein or similar) but, in its simplest form, activity refers to the contribution of a single enzyme molecule. The turnover number of an enzyme-substrate combination refers to the number of substrate molecules metabolized in unit time (usually a period of 1 s) under a given set of conditions (see later). These definitions appear, at first glance, to be largely self-explanatory. However, many factors contribute to the final activity of an enzyme, and these must be considered during any assessment of such activity. [Pg.96]

The observed adsorbate lattice structures show enantiomorphism, that is, adsorption of the right-handed P-heptahehcene (P stands for positive) leads to structures which are mirror images of those observed for M-heptahelicene. This effect can be clearly observed in the high-resolution STM images of Fig. 4.19. Furthermore, the enantiomeric lattices form opposite angles with respect to the [lIO] substrate surface direction. The combined molecule-substrate systems thus exhibit extended... [Pg.178]

The symmetry and height of the rotational barriers and hence the tunnel splittings depend strongly on the orientation of the molecule and its adsorption site. The results of these measurements (a higher resolution experiment is planned) when combined with model calculations based on empirical atom-atom potentials (see below) may be able to provide corroborative evidence for the orientation of an adsorbed molecule as well as details of the molecule-substrate interaction. The principal obstacle to a wider application of the technique may simply be the small number of adsorbed systems in which these tunnel splittings can be observed. [Pg.255]

In the formation of SAMs, the film-forming molecules order themselves by chemical interaction with neighbouring molecules and with the substrate surface. This technique has been applied for a large variety of modifier/substrate combinations. Various sulphur compounds, like alkanethiols and (di)sulfides have been deposited on metals such as silver, copper and gold isocyanides on platinum and carboxylic acids on aluminum oxide and silver oxide.75 Alkyltrichlorosilanes have been deposited on gold, mica, aluminum, tin oxide and silicon oxide. The latter combination is of interest here. [Pg.181]

The competition between molecular-based and molecule-substrate interactions is one of the features that make supramolecular assemblies based on the combination of molecular components and solid substrates so exciting and also potentially useful from the applications point of view. The control issue is whether can one achieve long-lived charge separation between molecular components when immobilized on a surface, and from the fundamental perspective, can the interactions between the surface and molecular components be manipulated In this section, the immobilization of molecular components consisting of at least two electroactive and/or photoactive units will be discussed. The intramolecular interactions within these dyads in solution, as well as their behavior as interfacial supramolecular triads when immobilized on nanocrystalline TiC>2, will be compared. [Pg.289]

Many substances interact with enzymes to lower their activity that is, to inhibit them. Valuable information about the mechanism of action of the inhibitor can frequently be obtained through a kinetic analysis of its effects. To illustrate, let us consider a case of competitive inhibition, in which an inhibitor molecule, I, combines only with the free enzyme, E, but cannot combine with the enzyme to which the substrate is attached, ES. Such a competitive inhibitor often has a chemical structure similar to the substrate, but is not acted on by the enzyme. For example, malonate (-OOCCH2COO-) is a competitive inhibitor of succinate (-OOCCH2CH2COO-) dehydrogenase. If we use the same approach that was used in deriving the Michaelis-Menten equation together with the additional equilibrium that defines a new constant, an inhibitor constant, A),... [Pg.98]

Previous research has also indicated that certain dyestuffs can react to particular external conditions and thus produce color changes. An overview of related research articles indicate that factors influencing color changes involve internal characteristics of the substrate and dye molecules in combination and external forces, such as light, humidity, heat, atmospheric contaminants, or other foreign substances introduced in wear and in cleaning processes (4,6,13,14,15). [Pg.273]

The main function of the ink is to bring a functional molecule, usually a colorant, to a substrate. If the colorant is a dye molecule (or combination of various molecules) it should be present at a concentration much below its solubihty limit, otherwise slight variations during storage (e.g., temperature, pH) could cause precipitation. In such inks it is essential to determine the dye solubility in presence of all the components, especially at low temperatures. The optical properties... [Pg.28]

These substrates combine a (3 )-substituent with a (3Z)-substituent in the same molecule. Allylic alcohols with only a (3 )-substituent generally are epoxidteed with excellent enantioselectivity, whereas those with only a (3Z substituent are epoxidized with enantioselectivity in the range of 80-95% ee. In tee combination many of tee reported examples have a methyl substituent at tee (3Z)-positi(Hi and all of these are epoxidized with an enantiomeric excess of 90-95% (Table 7, entries 1-4 and 6). Only a limited number of examples with larger groups at tee (3Z)-position have been reported (entries 5 and 7-12) and in these the enantiomeric excesses are in tee range 84-94%. [Pg.409]

At initial point, eventhough the substrate molecules are present in excess than enzyme on molar basis, not all the enzyme molecules present combine with the... [Pg.187]

When the inhibitor is added to the enzyme in the presence of its substrate, the reaction between the enzyme and inhibitor may be delayed because some of the enzyme molecules are combined with the substrate and are therefore protected from reacting with the inhibitor. However, as the substrate molecules react chemically, the active centers become available and inhibition will eventually become complete even though an excess of substrate may initially have been present. Furthermore, addition of more substrate is ineffective in reversing the inhibition in contrast to its effect on reversible competitive inhibition, which is discussed later. [Pg.206]

Even with this minimal scheme, it is clear that Km can be equated with the dissociation constant of the ES complex, K, only if k i k+2, i.e. the substrate comes off the enzyme many times for every occasion it is transformed or the commitment to catalysis (defined in Section 5.4.4.) is zero. On the other hand, if k i k+2, every molecule that binds to the enzyme is transformed, the substrate is said to be sticky , the commitment to catalysis is unity and k g JKm becomes equal to k+i, the rate of enzyme-substrate combination. This is usually the diffusion limit, so that absolute values of k mlKm approaching 10 s particularly if they do not vary with substrate, are a... [Pg.306]

Liquid-phase adsorption characteristics examined by atomic force microscopy (AFM) were compared for two pyridine base molecules, pyridine and d-picoline. on (010) surfaces of two natural zeolites, heulandite and stilbite. These adsorption systems formed well-ordered. two-dimensioncJ (quasi-)hexagonal adlayers. The 2D lattice structures of the ordered adlayers w ere dependent on the adsorbate/substrate combinations. Although there existed certain habit in the orientation of the 2D lattice unit vector of the adsorbed phase with respect to the substrate(OlO) lattice vectors, the molecular arrays w ere incommensurate with the substrate atomic arrangements. [Pg.185]

The specificity of the enzyme led to the postulate of a lock-and-key type of mechanism. The substrate molecule, by combining in a special way with the active site on the enzyme, is activated f or the reaction that it is to undergo. The active site on an enzyme may consist of more than one site on the protein molecule one site may attach to one part of the substrate molecule, while another site binds another part of the substrate molecule. The lock-and-key model seems to be generally correct, but the details of the action are different f or different enzymes. [Pg.836]


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Molecule substrate

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