The Protein Man's Blog | A Discussion of Protein Research

Proteins that form complexes tend to form aggregates during recombinant expression. So the best method is to co-express proteins with suitable partner protein. Chaperones are one of those proteins that help insoluble protein formation. Researchers observed the enhanced solubility of some proteins when co-expressed with chaperones. However, the choice of suitable chaperone for a particular protein is difficult to assume and only with trial and error methods one can achieve a soluble protein. Chaperones act as catalysts that prevent aggregation of nascent chains and unfolding aggregate proteins. Co-expression of recombinant proteins with chaperones help in improved solubility, enhanced specific activity and yield of target proteins.

Genomic DNA extraction is an important part of the process when it comes to studying DNA. Pure DNA, separated from the proteins and fluid of cells, is needed on its own in order to be used for various molecular applications. These analyses can include cloning, sequencing, electrophoresis, and fingerprinting.

In the radioimmunoassay, high specific radioactive antigens are used as tracers. Iodinated proteins are used to study hormonal interaction with target tissue and immunoglobulin metabolism. The chloramine-t procedure is the oldest method used to iodinate proteins and peptides directly with ¹²⁵ I, but it is observed that there is a loss of activity of proteins iodinated by this method. The disadvantage of this method is difficulty in iodination of proteins lacking tyrosine residues.