E. coli is most preferred system used for the production of recombinant proteins in bacteria
and the availability of improved genetic tools/methods are making it more valuable than …

Bionanotechnology has now become firmly established in its own right as one of the
principle and focused subdisciplines within nanotechnology.(1-10) Bionanotechnology can …

Proteins are now widely produced in diverse microbial cell factories. The Escherichia coli is
still the dominant host for recombinant protein production but, as a bacterial cell, it also has …

Protein semisynthesis—defined herein as the assembly of a protein from a combination of
synthetic and recombinant fragments—is a burgeoning field of chemical biology that has …

Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …

Protein fusion tags are indispensible tools used to improve recombinant protein expression
yields, enable protein purification, and accelerate the characterization of protein structure …

In response to the rapidly growing field of proteomics, the use of recombinant proteins has
increased greatly in recent years. Recombinant hybrids containing a polypeptide fusion …

A protein semisynthesis method—expressed protein ligation—is described that involves the
chemoselective addition of a peptide to a recombinant protein. This method was used to …

Addition of an affinity tag is a useful method for differentiating recombinant proteins
expressed in bacterial and eukaryotic expression systems from the background of total …

Fok I is a type IIs restriction endonuclease comprised of a DNA recognition domain and a
catalytic domain. The structural similarity of the Fok I catalytic domain to the type II restriction …