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)

Modification of isolated subunit c of the F1Fo-ATPase from Propionigenium modestum by dicyclohexylcarbodiimide.

Subunit c of the F1Fo-ATPase from Propionigenium modestum was extracted from the particulate cell fraction with chloroform/methanol. The protein was further purified by carboxymethyl cellulose chromatography and anion exchange HPLC in the organic solvent. SDS-PAGE of the purified protein indicated a single stained protein band migrating as expected for the c-subunit. Incubation of isolated subunit c in chloroform/methanol or aqueous buffer containing dodecyl-beta-D-maltoside with [14C]dicyclohexylcarbodiimide (DCCD) resulted in the incorporation of radioactivity into the protein. The rate of this reaction depended on the external pH; it was significantly faster in the more acidic than in the alkaline pH range. In the presence of Na+ subunit c was partially protected from labeling with [14C]DCCD at pH 6.1 and at pH 7.5, whereas no protection was evident at pH 5. 5. At pH 7.5, the rate of subunit c labeling by [14C]DCCD in the presence of 20 mM NaCl was about 50% lower than in the absence of Na+ ions. The isolated c-subunit therefore apparently retains in part the Na+ binding site which, when occupied, diminishes the reactivity of the protein towards DCCD.[1]


WikiGenes - Universities