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)

Identification of the second (buried) cysteine residue and of the C-terminal disulfide bridge of bovine spleen cathepsin B.

Quantitative differences were found when bovine spleen cathepsin B was subjected to SH-group titration in the presence and in the absence of denaturing agents, as well as when the pH of the titration buffer was increased. The intra- and interchain thiol-disulfide exchange reactions accompanying the denaturation of cathepsin B were investigated by polyacrylamide gel electrophoresis in SDS and by gel filtration experiments. An identical behavior in these experiments showed also cathepsin B whose active site Cys29 only had been carboxymethylated; these findings suggested the presence of one additional SH-group. After conditions preventing thiol-disulfide exchange reactions, had been developed, the second SH-group (Cys240) was demonstrated independently in carboxymethylated cathepsin B by labeling with 4-(dimethylamino)azobenzene-4'-iodoacetamide and by selective isolation of the SH-peptide containing Cys240 on thiopropyl-Sepharose. As the second important result, a disulfide bridge formed by Cys148 and Cys252 in the C-terminal part of the chain was identified.[1]


WikiGenes - Universities