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Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy. | LitMetric

Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy.

J Am Chem Soc

Magnetic Resonance Center and Department of Chemistry "Ugo Schiff", University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.

Published: October 2024

AI Article Synopsis

Article 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 N,H labeled and the interacting one being C,H-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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11523233PMC
http://dx.doi.org/10.1021/jacs.4c09176DOI Listing

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