ReviewProtein science : a publication of the Protein Society2017
(S)Pinning down protein interactions by NMR.
Review in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
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- Hierarchy in regulator interactions with distant transcriptional activation domains empowers rheostatic regulation.Protein science : a publication of the Protein Society · 2025Article
- DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2.Nature communications · 2024Article
- 2'-Frontiers in molecular biosciences · 2024Article
- Structural insight into EV-A71 3A protein and its interaction with a peptide inhibitor.Virologica Sinica · 2023Article
- Functional characterization of a lytic polysaccharide monooxygenase from Schizophyllum commune that degrades non-crystalline substrates.Scientific reports · 2023Article
- The C-terminal transactivation domain of MITF interacts promiscuously with co-activator CBP/p300.Scientific reports · 2023Article
- Phosphorylation of Schizosaccharomyces pombe Dss1 mediates direct binding to the ubiquitin-ligase Dma1 in vitro.Protein science : a publication of the Protein Society · 2023Article
- Ensemble determination by NMR data deconvolution.Nature reviews. Chemistry · 2023Review
- Following the Fate of Lytic Polysaccharide Monooxygenases under Oxidative Conditions by NMR Spectroscopy.Biochemistry · 2023Article
- Article
- Fully Automated Characterization of Protein-Peptide Binding by Microfluidic 2D NMR.Journal of the American Chemical Society · 2023Article
- Molecular insights into alginate β-lactoglobulin A multivalencies-The foundation for their amorphous aggregates and coacervation.Protein science : a publication of the Protein Society · 2023Article
- Biophysical Approaches for the Characterization of Protein-Metabolite Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Deciphering the Alphabet of Disorder-Glu and Asp Act Differently on Local but Not Global Properties.Biomolecules · 2022Article
- Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.International journal of molecular sciences · 2022Article
- Searching for the Best Transthyretin Aggregation Protocol to Study Amyloid Fibril Disruption.International journal of molecular sciences · 2021Article
- The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
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.
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