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Alcohol binding sites

KRUSE, S.W., ZHAO, R., SMITH, D.P., JONES, D.N.M., Structure of a specific alcohol-binding site defined by the odorant binding protein lush from Drosophila melanogaster. Nature Str. Biol, 2003,10, 694-700. [Pg.262]

Introduction of New Alcohol Binding Sites at the Lipid/Water Interface by the Incorporation of Monosialogangliosides into DPPC Liposomes... [Pg.1]

INTRODUCTION OF NEW ALCOHOL BINDING SITES AT THE LIPID/WATER INTERFACE BY THE INCORPORATION OF MONOSIALOGANGLIOSIDES INTO DPPC LIPOSOMES... [Pg.631]

Johjima, T., Wariishi, H., and Tanaka, H. (2002) Veratryl alcohol binding sites of lignin peroxidase from Phane-rochaete chrysosporium. /. Mol. Catal. B Enzym., 17, 49-57. [Pg.545]

Harris RA, Blednov Y, Findlay G et al (2001) Can a single binding site account for actions of alcohols on GABAa and glycine receptors Alcohol Clin Exp Res (5 Suppl) 79S-80S... [Pg.486]

The crystal structure of the HNL isolated from S. bicolor (SbHNL) was determined in a complex with the inhibitor benzoic acid." The folding pattern of SbHNL is similar to that of wheat serine carboxypeptidase (CP-WII)" and alcohol dehydrogenase." A unique two-amino acid deletion in SbHNL, however, is forcing the putative active site residues away from the hydrolase binding site toward a small hydrophobic cleft, thereby defining a completely different active site architecture where the triad of a carboxypeptidase is missing. [Pg.151]

Alkanes and short alcohols actually partition into the interior of the membrane [171]. The well-shielded tetraphenylphosphonium (TPP+) and tetraphe-nylborate (TPB-) ions are also deeply intercalated into the lipid bilayer [6,169]. The binding site of TPB- is located somewhere below the head-group region in the vicinity of the ester groups, while the cation TPP+ binds a few tenths of a nanometre further outwards [6],... [Pg.236]

Figure 1. Illustration of lone electron pair preferences in alcohol dimers, cooperative and anticooperative binding sites for a third monomer, ring strain and steric repulsion in alcohol trimers, alternation of residues in alcohol tetramers, and chain, branch, and cyclic hydrogen bond topologies in larger clusters. Figure 1. Illustration of lone electron pair preferences in alcohol dimers, cooperative and anticooperative binding sites for a third monomer, ring strain and steric repulsion in alcohol trimers, alternation of residues in alcohol tetramers, and chain, branch, and cyclic hydrogen bond topologies in larger clusters.
D. S. Dwyer and R. J. Bradley, Chemical properties of alcohols and their protein binding sites. Cell. Mol. Life Sci. 57, 265 275 (2000). [Pg.42]

As an example of the techniques/ Figure 4 shows a comparison of the fungicidally active RR- diclobutrazol with the natural substrate lanosterol. The sterol C-32 alcohol is chelated to the iron porphyrin. The three central features of the model cytochrome P-450 can be elucidated. The hydrophobic binding site, the polar region between this hydrophobic region and the heme plane/ and a common complexation to the porphyrin iron. [Pg.179]

Rhodium(II) forms a dimeric complex with a lantern structure composed of four bridging hgands and two axial binding sites. Traditionally rhodium catalysts faU into three main categories the carboxylates, the perfluorinated carboxylates, and the carboxamides. Of these, the two main bridging frameworks are the carboxylate 10 and carboxamide 11 structures. Despite the similarity in the bridging moiety, the reactivity of the perfluorinated carboxylates is demonstrably different from that of the alkyl or even aryl carboxylates. Sohd-phase crystal structures usually have the axial positions of the catalyst occupied by an electron donor, such as an alcohol, ether, amine, or sulfoxide. By far the most widely used rhodium] 11) catalyst is rhodium(II) acetate [Rh2(OAc)4], but almost every variety of rhodium] 11) catalyst is commercially available. [Pg.435]


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See also in sourсe #XX -- [ Pg.631 , Pg.632 , Pg.633 , Pg.634 , Pg.635 , Pg.636 , Pg.637 , Pg.638 ]




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Alcohols binding

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