Magnetic Resonance Access to Transiently Formed Protein Complexes |
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Authors: | Tomá? Sára Thomas C Schwarz Dennis Kurzbach Christoph H Wunderlich Christoph Kreutz Robert Konrat |
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Institution: | [a]Department of Structural and Computational Biology Max F. Perutz Laboratories, Vienna Biocenter Campus 5, 1030 Vienna (Austria), E-mail: ;[b]Institute of Organic Chemistry and CMBI, University of Innsbruck, Innrain 80/82, 6020 Innsbruck (Austria) |
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Abstract: | Protein–protein interactions are of utmost importance to an understanding of biological phenomena since non-covalent and therefore reversible couplings between basic proteins leads to the formation of complex regulatory and adaptive molecular systems. Such systems are capable of maintaining their integrity and respond to external stimuli, processes intimately related to living organisms. These interactions, however, span a wide range of dissociation constants, from sub-nanomolar affinities in tight complexes to high-micromolar or even millimolar affinities in weak, transiently formed protein complexes. Herein, we demonstrate how novel NMR and EPR techniques can be used for the characterization of weak protein–protein (ligand) complexes. Applications to intrinsically disordered proteins and transiently formed protein complexes illustrate the potential of these novel techniques to study hitherto unobserved (and unobservable) higher-order structures of proteins. |
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Keywords: | electron paramagnetic resonance intrinsically disordered proteins nuclear magnetic resonance protein– protein interactions transient complexes structure characterization of biomolecules |
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