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)

The sequence of a peptide containing the active site phosphohistidine residue of phosphoglycerate mutase from chicken breast muscle.

Phosphoglycerate mutase is phosphorylated on a histidine residue by the cofactor of the reaction, 2,3-bisphosphoglycerate (Rose, Z. B. (1970) Arch. Biochem. Biophys. 140, 508-513). The phosphoryl group is readily transferred to the normal acceptors, 3-phosphoglycerate and 2-phosphoglycerate, or to water in the presence of glycolate-2-P. An acid-labile phosphorylated decapeptide has been purified from a tryptic digest of the phosphoenzyme. The amino acid sequence of the peptide has been determined to be: Aal-Gly-Gln-Leu-Asp-Glu-Ser-His-Arg. This sequence bears a striking analogy to part of a highly conserved region of lactate dehydrogenase (residues 100 to 109) (Taylor, S. S., Oxley, S. S., Allison, W. S., and Kaplan, N. O. (1973) Proc. Natl. Acad. Sci. U. S. A. 70, 1970-1974). Evidence from x-ray crystallographic studies indicates that the two enzymes are similar in tertiary structure (Campbell, J. W., Watson, H. C. and Hodgson, G. I. (1974) Nature 250, 301-303).[1]


WikiGenes - Universities