Described in this unit are five basic protocols that are widely used for specific and efficient
chemical cleavage of proteins in solution. Cyanogen bromide (CNBr) cleaves at methionine …

The genetic modification of recombinant proteins to include affinity tags can greatly simplify
their purification. A key drawback to this technology has been the difficulty and expense …

In the affinity purification of recombinant fusion proteins, the rate-limiting step is usually the
efficient proteolytic cleavage and removal of the affinity tail and the protease from the …

The efficient removal of a N-or C-terminal purification tag from a fusion protein is necessary
to obtain a protein in a pure and active form, ready for use in human or animal medicine …

Characterizing the movement, interactions, and chemical microenvironment of a protein
inside the living cell is crucial to a detailed understanding of its function. Most strategies …

Peptide cyclization is a useful strategy for the stabilization of short flexible peptides into well-
defined bioactive conformations, thereby enhancing their ability to interact with proteins and …

Although they are often exploited to facilitate the expression and purification of recombinant
proteins, every affinity tag, whether large or small, has the potential to interfere with the …

Overproduction of proteins from cloned genes using fusion protein expression vectors in
Escherichia coli and eukaryotic cells has increased the quantity of protein produced. This …

This unit provides protocols for some commonly used methods of site‐specific cleavage of
fusion proteins. The first three protocols describe enzymatic cleavage of proteins using …

Chemical ligation of unprotected peptides has enabled the successful synthesis of a large
number of diverse proteins.[1] The native chemical ligation (NCL) reaction,[2] which …