|Nature Biotechnology (2001) 19(2):131-6|
|Northeast Structural Genomics Consortium|
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Protein misfolding is the basis of a number of human diseases and presents an obstacle to the production of soluble recombinant proteins. ...
We present a general method to assess the solubility and folding of proteins in vivo. The basis of this assay is structural complementation between the alpha- and omega- fragments of beta-galactosidase (beta-gal). Fusions of the alpha-fragment to the C terminus of target proteins with widely varying in vivo folding yield and/or solubility levels, including the Alzheimer's amyloid beta (A beta) peptide and a non-amyloidogenic mutant thereof, reveal an unambiguous correlation between beta-gal activity and the solubility/folding of the target. Thus, structural complementation provides a means of monitoring protein solubility/misfolding in vivo, and should find utility in the screening for compounds that influence the pathological consequences of these processes.
|chemistry genetics metabolism |
|Genes, Reporter Cystic Fibrosis Transmembrane Conductance Regulator Humans Solubility Mutagenesis, Site-Directed Recombinant Fusion Proteins Genetic Markers Protein Folding Amyloid beta-Peptides beta-Galactosidase Peptide Fragments |
|119 (Last update: 04/01/2017 12:18:29pm)|
|Nat Biotechnol. 2001 Feb;19(2):131-6.|