By a News Reporter-Staff News Editor at Science Letter -- Data detailed on Peptides and Proteins have been presented. According to news reporting originating in Toronto, Canada, by NewsRx journalists, research stated, "SDS/PAGE is universally used in biochemistry, cell biology, and immunology to resolve minute protein amounts readily from tissue and cell extracts. Although molecular weights of water-soluble proteins are reliably determined from their SDS/PAGE mobility, most helical membrane proteins, which comprise 20-30% of the human genome and the majority of drug targets, migrate to positions that have for decades been unpredictably slower or faster than their actual formula weight, often confounding their identification."
The news reporters obtained a quote from the research from the University of Toronto, "Using de novo designed transmembrane-mimetic polypeptides that match the composition of helical membrane-spanning sequences, we quantitate anomalous SDS/PAGE fractionation of helical membrane proteins by comparing the relative mobilities of these polypeptides with typical water-soluble reference proteins on Laemmli gels. We find that both the net charge and effective molecular size of the migrating particles of transmembrane-mimetic species exceed those of the corresponding reference proteins and that gel acrylamide concentration dictates the impact of these two factors on the direction and magnitude of anomalous migration. Algorithms we derived from these data compensate for this differential effect of acrylamide concentration on the SDS/PAGE mobility of a variety of natural membrane proteins."
According to the news reporters, the research concluded: "Our results provide a unique means to predict anomalous migration of membrane proteins, thereby facilitating straightforward determination of their molecular weights via SDS/PAGE."
For more information on this research see: Acrylamide concentration determines the direction and magnitude of helical membrane protein gel shifts. Proceedings of the National Academy of Sciences of the United States of America, 2013;110(39):15668-15673. Proceedings of the National Academy of Sciences of the United States of America can be contacted at: Natl Acad Sciences, 2101 Constitution Ave NW, Washington, DC 20418, USA. (National Academy of Sciences - www.nasonline.org/; Proceedings of the National Academy of Sciences of the United States of America - www.nasonline.org/publications/pnas/)
Our news correspondents report that additional information may be obtained by contacting A. Rath, University of Toronto, Dept. of Biochem, Toronto, ON M5S 1A8, Canada. Additional authors for this research include F. Cunningham and C.M. Deber (see also Peptides and Proteins).
Keywords for this news article include: Canada, Toronto, Ontario, Acrylates, Acrylamides, Amino Acids, Carboxylic Acids, Membrane Proteins, Organic Chemicals, Peptides and Proteins, North and Central America
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