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)

Structure of the proteolipid protein extracted from bovine central nervous system myelin with nondenaturing detergents.

As a basis for attempts to define the structures of the proteins within myelin, methods have been developed for their extraction and isolation in solutions of non-denaturing detergents. With use of solutions of deoxycholate or Triton X-100, up to 90% of the protein has been extracted from bovine CNS myelin, along with most of the phospholipid. The proteolipid protein has been purified in deoxycholate solutions by chromatography on a blue dye-ligand column, which retained all of the basic protein and 2',3'-cyclic nucleotide-3'-phosphodiesterase, and then on Sephacryl S300, which separated proteolipid protein from phospholipid and high-molecular-weight proteins. The proteolipid protein was isolated from Triton X-100 extracts of myelin by adsorption onto phosphocellulose resin, with subsequent elution by 0.5 M sodium chloride. Gel permeation chromatography was used as the final purification step. Sedimentation equilibrium experiments gave a monomer molecular weight of 134,000 +/- 8000 in deoxycholate and 145,000 +/- 17,000 in Triton X-100 solutions. On the basis of an apparent subunit molecular weight of 23,500 it was deduced that the native protein is probably hexameric. Above 0.2 gL-1 in Triton X-100 solutions and 0.5 gL-1 in deoxycholate solutions the protein aggregated. In deoxycholate solutions the protein adopts the highly helical conformation expected for an intrinsic membrane protein.[1]


WikiGenes - Universities