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

  In a previous blog article, we discussed western blotting technique and advancement in Western blot detection using fluorescence, not only fluorescence allows detection of multiple protein bands on the same blot (multiplexing) but is a more sensitive and reliable method of detection. The linear dynamic range of chemiluminescence is 10 times smaller than Fluorescence. This blog article focuses on one of the most useful and widely used applications of Western blotting, the quantitative western blotting. Quantitative western blotting combines western blotting with digital image analysis and allows molecular cell biologists to measure and quantify changes in protein abundance and modifications (Proteolysis and post-translational modifications).

Perhaps the most effective weapon in the fight against SARS CoV-2 will be the deployment of inexpensive, rapid diagnostic tests. The conventional testing requires the nasopharyngeal swabs taken as samples from patients or sample providers, followed by extraction of viral RNA and detection by RT-qPCR. This procedure is lengthy, offers low sensitivity during early infection and due to increase in demand and testing, the swabs and other raw materials required for viral nucleic acid extraction have become limited or nearly exhausted. Furthermore, the procedure of taking nasopharyngeal swab is invasive and may lead to coughing in some patients which increases the risk of nosocomial spread of virus.

How Chaperone-Assisted Protein Folding Works

What are chaperone-assisted proteins and what roles do they play in protein folding? Basically, chaperones are a group of proteins essential for promoting cell viability and stability. Thus, they are also responsible for ensuring that various processes such as translocation, degradation, and folding are carried out properly at all times.