NMR Spectroscopy of supramolecular chemistry on protein surfaces

Peter Bayer; Anja Matena; Christine Beuck

doi:10.3762/bjoc.16.203

NMR Spectroscopy of supramolecular chemistry on protein surfaces

Beilstein J Org Chem. 2020 Oct 9:16:2505-2522. doi: 10.3762/bjoc.16.203. eCollection 2020.

Authors

Peter Bayer¹, Anja Matena¹, Christine Beuck¹

Affiliation

¹ Structural and Medicinal Biochemistry, University of Duisburg-Essen, Universitätsstr. 1-5, 45141 Essen, Germany.

Abstract

As one of the few analytical methods that offer atomic resolution, NMR spectroscopy is a valuable tool to study the interaction of proteins with their interaction partners, both biomolecules and synthetic ligands. In recent years, the focus in chemistry has kept expanding from targeting small binding pockets in proteins to recognizing patches on protein surfaces, mostly via supramolecular chemistry, with the goal to modulate protein-protein interactions. Here we present NMR methods that have been applied to characterize these molecular interactions and discuss the challenges of this endeavor.

Keywords: NMR; molecular recognition; protein ligand interaction; protein surfaces; supramolecular chemistry.

Publication types

Review

Grants and funding

We gratefully acknowledge the Collaborative Research Centre CRC 1093 by the Deutsche Forschungsgemeinschaft for its support of our research on supramolecular chemistry on proteins.