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Using T4 genetics and Laemmli’s development of high-resolution SDS gel electrophoresis to reveal structural protein interactions controlling protein folding and phage self-assembly
Journal of Biological ChemistryVol. 298Issue 10102463Published online: September 3, 2022- Jonathan King
Cited in Scopus: 0One of the most transformative experimental techniques in the rise of modern molecular biology and biochemistry was the development of high-resolution sodium dodecyl sulfate polyacrylamide gel electrophoresis, which allowed separation of proteins—including structural proteins—in complex mixtures according to their molecular weights. Its development was intimately tied to investigations of the control of virus assembly within phage-infected cells. The method was developed by Ulrich K. Laemmli working in the virus structural group led by Aaron Klug at the famed Medical Research Council Laboratory for Molecular Biology at Cambridge, UK.