News
Latest addition : 18 June.
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Practical Course on High Throughput Recombinant Protein Production for Protein-Protein and Protein-Nucleic Acid Complexes
18 June -
To Fold or to Refold? A Shakespearean question applied to recombinant proteins.2 April 2012, bySince a majority of recombinant proteins are expressed in E. coli as inclusion bodies, in vitro refolding of denatured proteins can be a way to rescue them. To that aim, a refolding screen using 96 refolding buffers has been set up at AFMB and validated with 24 proteins, 70% of which remaining soluble in at least one buffer...
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Weakening mRNA secondary structures at the Ribosome Binding Site (RBS) can improve protein expression yields in E. coli.2 April 2012, bySchematic representation of the process performed by ExEnSo Recombinant protein translation in Escherichia coli may be limited by stable (i.e. low free energy) secondary structures in the mRNA translation initiation region. To circumvent this issue in the context of recombinant protein expression for Structural Genomics, we have developed a computer tool called ‘ExEnSo’ (Expression Enhancer Software) to perform “in silico” directed evolution. In a first step, ExEnSo generates a random library (...)
