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)
 
 
 
 
 Pirkl,  
 

Three-step purification of a fragment of the large immunophilin FKBP52.

PPIases catalyze the interconversion of cis and trans isomers of peptidyl-prolyl (Xaa-Pro) bonds in peptide and protein substrates. The PPIase family comprises three subfamilies, two of which interact with immunosuppressant drugs and are therefore termed immunophilins. One subgroup of the immunophilins are the FK506 binding proteins (FKBPs). FKBPs of a relative molecular mass higher than 40 000 also display chaperone activity and are part of the multichaperone complex that Hsp90 forms with substrate proteins. Their function in this chaperone complex is still enigmatic. To further characterize the function of FKBP52 we want to analyze constructs of FKBP52-fragments. Here we describe a fast and effective three-step purification procedure for a fragment of FKBP52 with a relative molecular mass of 48000, termed FKBP52-123, consisting of affinity chromatography, anion-exchange column and gel-permeation chromatography. A yield of 1 mg pure protein per gram of cells was achieved.[1]

References

  1. Three-step purification of a fragment of the large immunophilin FKBP52. Pirkl, F. J. Chromatogr. B Biomed. Sci. Appl. (2000) [Pubmed]
 
WikiGenes - Universities