(S)Pinning down protein interactions by NMR. (14th February 2017)

• Record Type: Journal Article
• Authors: Teilum, Kaare; Kunze, Micha Ben Achim; Erlendsson, Simon; Kragelund, Birthe B.
• Is Part Of: Protein science. Volume 26:Number 3(2017)
• Page Start: 436
• Page End: 451
• Publication Date: 2017-02-14
• Subjects: affinity -- dissociation constant -- spectroscopy -- ligand -- chemical shift -- binding -- exchange; Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.3105
• Languages: English
• ISSNs: 0961-8368

Abstract

Abstract: Protein molecules are highly diverse communication platforms and their interaction repertoire stretches from atoms over small molecules such as sugars and lipids to macromolecules. An important route to understanding molecular communication is to quantitatively describe their interactions. These types of analyses determine the amounts and proportions of individual constituents that participate in a reaction as well as their rates of reactions and their thermodynamics. Although many different methods are available, there is currently no single method able to quantitatively capture and describe all types of protein reactions, which can span orders of magnitudes in affinities, reaction rates, and lifetimes of states. As the more versatile technique, solution NMR spectroscopy offers a remarkable catalogue of methods that can be successfully applied to the quantitative as well as qualitative descriptions of protein interactions. In this review we provide an easy‐access approach to NMR for the non‐NMR specialist and describe how and when solution state NMR spectroscopy is the method of choice for addressing protein ligand interaction. We describe very briefly the theoretical background and illustrate simple protein–ligand interactions as well as typical strategies for measuring binding constants using NMR spectroscopy. Finally, this review provides examples of caveats of the method as well as the options to improve the outcome of an NMR analysis of a protein interaction reaction.