General information of database
|Solubility database of all E.coli proteins|
|Protein sequence databases - Protein properties|
The database of solubilities and synthetic yields of all E.coli proteins translated by using an in vitro reconstituted translation system. For 788 aggregation-prone proteins, the data of chaperone effects on the prevention of aggregate formation were added on May 2012.
Gene segments from plasmids of ASKA library (Kitagawa et al. 2005) , which is the library of all genes of the E. coli strain K-12, were amplified by PCR, and their proteins were synthesized by using an in vitro translation system (PURE system). The solubilities were evaluated by SDS-PAGE and autoradiography before and after centrifugation.
For aggregation-prone proteins (defined as the proteins with less than 30% solubility in the absence of any chaperone), observations of changes in solubility were made by adding the major chaperones of E. coli, Trigger Factor (TF), DnaK/DnaJ/GrpE (KJE) and GroEL/ES (GroE), individually.
Since PURE system is a reconstituted chaperone-free translation system, it is possible to evaluate the solubilities of translated proteins and the chaperone effects accurately. The acquired data will form the basis of protein folding studies and be useful for planning researches and industries using protein expression and improving their efficiencies.
Original website information
The Targeted Proteins Research Program promoted by the MEXT