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Surface binding

For an exhaustive list of complexes whose interaction with DNA has been examined, the reader should refer to Table 2 several compounds are also described in [65]. [Pg.42]

Complexes with less extended aromaticity such as Ru(bpy/phen)2HAT [73-76] (HAT = 1,4,5,8,9,12-hexaazatriphenylene, Fig, 2) and Ru(bpy)2PPZ [77-80] (PPZ = 4,7-phenanthrolino-[6,5-b] pyrazine. Fig. 2) exhibit also characteristics most relevant to intercalation. We can mention (1) a very slow mobility of the HAT complex along the DNA double helix [81], (2) a good protection of the complex versus reagents that remain in the bulk solution [73,79], and (3) a clear hypochromic effect on the MLCT transition in the presence of DNA [73, 75, 79,80]. [Pg.45]

The values of the binding constants determined with different salt concentrations by equilibrium dialyses [43, 48], luminescence titrations and electrochemiluminescence [82], are all 2 or 3 orders of magnitude lower than for ethidium bromide. Therefore, a priori, they do not indicate contribution of classical intercalation into DNA as described for organic molecules and for the DPPZ, HAT and PPZ complexes. [Pg.46]

The results and observations from the experimental methods used to study the interaction modes of RuCphen) are compiled in Table 1. The examination of this table indicates obvious disagreements between the authors concerning the intercalation of Ru(phen)3 into DNA. Chronologically, the first spectroscopic experiments (entries 1 to 4) and the first results on DNA unwinding and dcnaturation (entries 11,12) in 1984-1986 were all consistent with intercalation. Afterwards, with the results from LD and NMR in 1988-1992 (entries 5, 7) and with the viscosity measurements in 1992 (entry 10), the intercalation of Rufphen) has become questionable. [Pg.46]

Thus on the one hand, from a series of approaches (entries 1-4,6-8,11), Barton and co-workets describe 3 modes of binding for this complex, some of them with enantiomeric selectivity  [Pg.46]


The material factor A contains the material parameters and is a description of the number of recoil atoms that can escape from the soUd. In one description (31) (eq. 18), N is the atomic density of target atoms and is the surface binding energy. [Pg.395]

When an impacting particle transfers energy to a near sinface carbon atom in an amount sufficient to overcome the lattice bond energy or surface binding energy, some carbon atoms may be displaced and move in a direction defined by the angle... [Pg.412]

Milligan, R.A., Whittaker, M., Safer, D. (1990). Molecular structure of F-actin and location of surface binding sites. Nature 248,217-221. [Pg.57]

O2, Mn, pH, and solid concentrations indicates that the character of the solid is important partly because some surfaces bind Mn " more strongly and partly because they facilitate the electron transfer differently. Catalysis by enzymes is clearly the most effective oxidation enhancing process as indicated by the laboratory studies with spores and material from the O2/H2S interface of Saanich Inlet. Microbial catalysis in this environment reduces the oxidation lifetime of Mn to about one day. This example illustrates... [Pg.433]

Wiggins RC. Bouma BN. Cochrane CG. Griffin JH Role of high-molecular-weight kininogen in surface-binding and activation of coagulation factor XI and prekallikrein. Proc Natl Acad Sci USA 1977 74 4636-4640. [Pg.81]

In this section, the surface chemistry of non-metals adsorbed as thin layers, films or SAMs on gold surfaces is discussed. Although attachment by a sulfur atom is by far the most predominant binding motif, many other elements may be used to bind to gold. Particular focus is given here to surface binding through atoms other than those already extensively covered in the literature. [Pg.335]

The idea of ligand efficiency was extended by considering other molecular descriptors. Abad-Zapatero and Metz [56] introduced a percentage efficiency index, a binding efficiency index and a surface-binding efficiency index by normalizing... [Pg.451]

Radoff, S., Vlassara, H. and Cerami, A. (1988). Characterisation of a solubilised cell surface binding protein on macrophages specific for proteins modified non-enzymatically by advanced... [Pg.197]

Usually adsorption, i.e. binding of foreign particles to the surface of a solid body, is distinguished as physical and chemical the difference lying in the type of adsorbate - adsorbent interaction. Physical adsorption is assumed to be a surface binding caused by polarization dipole-dipole Van-der-Vaals interaction whereas chemical adsorption, as any chemical interaction, stems from covalent forces with plausible involvement of electrostatic interaction. In contrast to chemisorption in which, as it has been already mentioned, an absorbed particle and adsorbent itself become a unified quantum mechanical system, the physical absorption only leads to a weak perturbation of the lattice of a solid body. [Pg.13]

Functional group protein Functional group surface binding... [Pg.492]

In the EIPET boundary condition, the electrochemical reduction of electro-active ions adsorbed on the particle provides the essential surface binding interaction which is responsible for particle deposition on the electrode surface. The particle flux is given by... [Pg.216]

Krivan HC, Clark GF, Smith DF, Wilkins TD Cell surface binding site for Clostridium difficile enterotoxin Evidence for a glycoconjugate containing the sequence Gal alpha l-3Galbeta l-4GlcNAc. Infect Immun 1986 53 573-581. [Pg.33]

The classic cadherins are homophilic adhesion molecules. That is, E-cadherin expressed on one cell surface binds to E-cadherin expressed on an apposed cell surface, N-cadherin binds to N, P to P and so forth. It was originally thought that all cadherins would behave completely homophilically but it is now clear that, for example, N-cadherin can bind to R-cadherin, although perhaps more weakly than it would to N-cadherin. [Pg.115]

Describe the surface features, with particular reference to orbital availability, involved in surface binding of components in soil. [Pg.82]


See other pages where Surface binding is mentioned: [Pg.694]    [Pg.85]    [Pg.19]    [Pg.705]    [Pg.70]    [Pg.13]    [Pg.172]    [Pg.260]    [Pg.299]    [Pg.86]    [Pg.227]    [Pg.103]    [Pg.250]    [Pg.200]    [Pg.8]    [Pg.258]    [Pg.258]    [Pg.72]    [Pg.78]    [Pg.206]    [Pg.207]    [Pg.215]    [Pg.236]    [Pg.438]    [Pg.237]    [Pg.251]    [Pg.310]    [Pg.388]    [Pg.302]    [Pg.309]    [Pg.276]    [Pg.373]    [Pg.492]    [Pg.318]   
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See also in sourсe #XX -- [ Pg.541 ]

See also in sourсe #XX -- [ Pg.16 ]




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A Key Question - Does the Molecule Intercalate or Surface Bind

Adsorbate surface binding geometries

Binding interaction, surface relaxation

Binding of H2 to Bare Metal Atoms, Ions, and Surfaces

Binding of Proteins and Probes to Artificial Surfaces

Binding surface density

Cell surface binding proteins, identification

Cell surface, receptor/ligand binding

Cell-surface carbohydrate recognition binding

Collagen cell surface binding

Covalent Binding to Activated Nonactivated Surfaces

Equilibrium binding constant surface concentration

Gene delivery system surface binding systems

Ligand binding assay surface plasmon resonance

Ligand binding surface complementarity

Ligand-receptor Binding Surface

Localized surface plasmon resonance binding

Metal-surface binding

Oxide surfaces, metal binding

Particle surface site-binding model

Probe molecules surface binding

Protein binding, biomaterial surface

Receptor Determination DHP Binding Sites on Surface Membranes

Signaling pathways binding, cell surface receptors

Soil, lead surface binding

Surface Plasmon Resonance Binding Assays

Surface binding hypothesis

Surface binding model

Surface complexation models electrolyte-binding constants

Surface plasmon resonance antigen-antibody binding

Surface structure, binding energy

Surface-exposed binding sites

Surfaces Tight-Binding Approximation

Surfaces Universal Binding Energy Relation

Surfaces binding energy

Surfaces protein binding

The Relative Free Energy Surface of 1,6-DHN Binding

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