ArticleMethods in enzymology2019
Characterization of Internal Protein Dynamics and Conformational Entropy by NMR Relaxation.
Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- NMR relaxation dispersion reveals an order of magnitude range of acid loop motions in protein tyrosine phosphatase 1B.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Direct Determination of Protein Rotational Diffusion Tensors and Generalized Order Parameters from MultifieldJournal of the American Chemical Society · 2026Article
- A steady-state approach for analysis of high-resolution relaxometry.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Pitfalls in measurements of RJournal of biomolecular NMR · 2025Article
- Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers.Journal of biomolecular NMR · 2024Article
- Insight into the autoproteolysis mechanism of the RsgI9 anti-σ factor from Clostridium thermocellum.Proteins · 2024Article
- Uremic Toxin-Induced Exosome-like Extracellular Vesicles Contain Enhanced Levels of Sulfated Glycosaminoglycans which Facilitate the Interaction with Very Small Superparamagnetic Iron Oxide Particles.International journal of molecular sciences · 2023Article
- Pressure, motion, and conformational entropy in molecular recognition by proteins.Biophysical reports · 2023Article
- ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.Science advances · 2022Article
- Computational study on the allosteric mechanism ofComputational and structural biotechnology journal · 2021Article
- RING NMR dynamics: software for analysis of multiple NMR relaxation experiments.Journal of biomolecular NMR · 2021Article
- Analysis of conformational exchange processes using methyl-TROSY-based Hahn echo measurements of quadruple-quantum relaxation.Magnetic resonance (Gottingen, Germany) · 2021Article
- DynamicJournal of biomolecular NMR · 2020Article
- Protein conformational entropy is not slaved to water.Scientific reports · 2020Article
- Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.Angewandte Chemie (International ed. in English) · 2020Article
- Opportunities and Challenges of Backbone, Sidechain, and RDC Experiments to Study Membrane Protein Dynamics in a Detergent-Free Lipid Environment Using Solution State NMR.Frontiers in molecular biosciences · 2019Review
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7 authors.
Funding
Abstract
Recent studies suggest that the fast timescale motion of methyl-bearing side chains may play an important role in mediating protein activity. These motions have been shown to encapsulate the residual conformational entropy of the folded state that can potentially contribute to the energetics of protein function. Here, we provide an overview of how to characterize these motions using nuclear magnetic resonance (NMR) spin relaxation methods. The strengths and limitations of several techniques are highlighted in order to assist with experimental design. Particular emphasis is placed on the practical aspects of sample preparation, data collection, data fitting, and statistical analysis. Additionally, discussion of the recently refined "entropy meter" is presented and its use in converting NMR observables to conformational entropy is illustrated. Taken together, these methods should yield new insights into the complex interplay between structure and dynamics in protein function.
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