title: Magnetic resonance access to transiently formed protein complexes.
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.
authors: Department of Structural and Computational Biology Max F. Perutz Laboratories Vienna Biocenter Campus 5, 1030 Vienna (Austria) E-mail: robert.konrat@univie.ac.at.
authors: Tomáš
authors: T
authors: Sára
authors: Department of Structural and Computational Biology Max F. Perutz Laboratories Vienna Biocenter Campus 5, 1030 Vienna (Austria) E-mail: robert.konrat@univie.ac.at.
authors: Thomas C
authors: TC
authors: Schwarz
authors: Department of Structural and Computational Biology Max F. Perutz Laboratories Vienna Biocenter Campus 5, 1030 Vienna (Austria) E-mail: robert.konrat@univie.ac.at.
authors: Dennis
authors: D
authors: Kurzbach
authors: Institute of Organic Chemistry and CMBI, University of Innsbruck Innrain 80/82, 6020 Innsbruck (Austria).
authors: Christoph H
authors: CH
authors: Wunderlich
authors: Institute of Organic Chemistry and CMBI, University of Innsbruck Innrain 80/82, 6020 Innsbruck (Austria).
authors: Christoph
authors: C
authors: Kreutz
authors: Department of Structural and Computational Biology Max F. Perutz Laboratories Vienna Biocenter Campus 5, 1030 Vienna (Austria) E-mail: robert.konrat@univie.ac.at.
authors: Robert
authors: R
authors: Konrat
keywords: electron paramagnetic resonance; intrinsically disordered proteins; nuclear magnetic resonance; protein–protein interactions; structure characterization of biomolecules; transient complexes