Received: Accepted: AugPublished: August 26, 2016Ĭopyright: © 2016 Hristozova et al. Brodsky, University of Pittsburgh, UNITED STATES The use of this method may lead to a considerable increase in the number of experimentally verified proteins with such functions, and may also allow the dissection of their molecular mechanism for a better understanding of their function.Ĭitation: Hristozova N, Tompa P, Kovacs D (2016) A Novel Method for Assessing the Chaperone Activity of Proteins. The current state of the art does not allow the in vitro measurements of chaperone activity in a highly parallel manner with high accuracy or high reproducibility, thus we believe that the method we report will be of significant benefit in this direction. Here we propose a novel technique to test and measure the capability for protective activity of known and putative chaperones in a semi-high throughput manner on a plate reader. Their molecular functions range from stabilizing stress-susceptible molecules and membranes to assisting the refolding of stress-damaged proteins, thereby acting as protective barriers against cellular damage. Among stress protein families–molecules expressed during adverse conditions, infection, and diseases–chaperones are highly abundant. Depending on their specific function, molecular chaperones are involved in a plethora of cellular processes by playing key roles in nascent protein chain folding, transport and quality control. Protein chaperones are molecular machines which function both during homeostasis and stress conditions in all living organisms.
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