Sonja Knödlstorfer, Marco Schiavina, Maria Anna Rodella, Karin Ledolter, Robert Konrat, Roberta Pierattelli, Isabella C. Felli
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引用次数: 0
Abstract
Intrinsically disordered proteins are abundant in eukaryotic systems, but they remain largely elusive pharmacological targets. NMR spectroscopy proved to be a suitable method to study these proteins and their interaction with one another or with drug candidates. Although NMR can give atomistic information about these interplays, molecular complexity due to severe spectral overlap, limited sample stability, and quantity remain an issue and hamper widespread applications. Here, we propose an approach to simultaneously map protein–protein binding sites onto two interacting partners by employing a complementary isotope-labeling strategy and a multiple receiver NMR detection scheme. With one partner being 15N,2H labeled and the interacting one being 13C,1H-labeled, we exploited proton and carbon detection to obtain clean and easily readable information. The method is illustrated with an application to the 50 kDa ternary protein complex formed between the prominent oncogenic transcription factor complex Myc/MAX and the tumor suppressor BRCA1.
期刊介绍:
The flagship journal of the American Chemical Society, known as the Journal of the American Chemical Society (JACS), has been a prestigious publication since its establishment in 1879. It holds a preeminent position in the field of chemistry and related interdisciplinary sciences. JACS is committed to disseminating cutting-edge research papers, covering a wide range of topics, and encompasses approximately 19,000 pages of Articles, Communications, and Perspectives annually. With a weekly publication frequency, JACS plays a vital role in advancing the field of chemistry by providing essential research.