Review List

  • Protein refolding (Chen)
    Proteins expressed in E. coli are often found as insoluble aggregates in inclusion body. It may be possible to increase the solubility for some porteins by reducing incubating temperature during protein expression, use of fusion partners such as GST, thioredoxin and maltose-binding protein, co-expression of chaperones etc.
    http://www.biochem.ucl.ac.uk/~chen/protocols/refol...
    Added: Tue May 14 2002, Hits: 3427, Reviews: 1 Read reviews  Write review  

    • 11 of 37 people found the following review helpful:
    Good but I've got a problem, Sat Nov 16 2002
    Reviewed By: Ding
    I found 1M Arg or NDSB201 is only partly dissolved (there is some NDSB201 precipitation) in the refolding buffer at 4C. Is this OK for protein refolding? Won't the undissolved Arg or DNSB201 particles facilitate the precipitation of the denatured protein? I just want to lower the NDSB concentration to make it completely soluable. What a concentration you would recommend? Thanks

    Was this review helpful to you?    

    Review Summary

    100% Times: 0 Times: 0 Times: 0 Times: 1 Times: 0
    80%
    60%
    40%
    20%
    0%
    Times  0 0 0 1 0
    Rating  1 2 3 4 5

    Add your own Review!