The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.
wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Mammalian 3-oxosteroid delta4-delta5-isomerase: a membrane-bound enzyme. I. Fluorescence study of the relationship between the enzymatic binding site, phospholipids, water and ions.
The microsomal membranes and the proteolipidic particles obtained by disruption of the microsomes by alkaline-earth ions at molar concentration have been compared by measuring the fluorescence properties of 1-anilino-naphthalene-3-sulfonate and naphthyl-1-phenylamine. The protein lipid arrangement of these two systems appears to be not essentially different. The study of fluorescence polarization of an hydrophobic probe (perylene) in function of Mg2+ concentration suggests a possible mechanism of disruption of the membrane by Mg2+ involving the strong structure-making effect of the ion. The comparison of the fluorescence polarization changes of perylene and equilenine (a competitive inhibitor of the isomerase) with the ionic concentration indicates that there is no direct relation between the bulk lipidic phase and the enzymatic binding site properties. Moreover, the emission of equilenine is completely quenched by I-, in contrast with the napththyl-1-phenylamine and perylene probes, which clearly demonstrates the accessibility of the catalytic site to water molecules and ions.[1]
