ArticleJournal of the American Chemical Society2020
Quantitative Interpretation of Solvent Paramagnetic Relaxation for Probing Protein-Cosolute Interactions.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Article
- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- A flexible, allosteric loop regulates protein activity and rewires electrostatics.Protein science : a publication of the Protein Society · 2025Article
- Modulation of histone tail electrostatic potentials in nucleosome core particles by acetylation and PARylation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Quantitative Interpretation of Transverse Spin Relaxation by Translational Diffusion in Liquids.The journal of physical chemistry. B · 2025Article
- Distinct association of HRAS and KRAS with MnMagnetic resonance letters · 2025Article
- Gadolinium-Based NMR Spin Relaxation Measurements of Near-Surface Electrostatic Potentials of Biomolecules.Journal of the American Chemical Society · 2024Article
- Observation of pH-Dependent Residual Structure in the Pmel17 Repeat Domain and the Implication for Its Amyloid Formation.Biochemistry · 2023Article
- Direct measurements of biomolecular electrostatics through experiments.Current opinion in structural biology · 2023Review
- Extending the Experimentally Accessible Range of Spin Dipole-Dipole Spectral Densities for Protein-Cosolute Interactions by Temperature-Dependent Solvent Paramagnetic Relaxation Enhancement Measurements.The journal of physical chemistry. B · 2023Article
- Interpreting Transient Interactions of Intrinsically Disordered Proteins.The journal of physical chemistry. B · 2023Article
- Identification of the Allosteric Binding Site for Thiazolopyrimidine on the C-Type Lectin Langerin.ACS chemical biology · 2022Article
- Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Inversion of HyperpolarizedThe journal of physical chemistry. B · 2022Article
- Assessment of the Components of the Electrostatic Potential of Proteins in Solution: Comparing Experiment and Theory.The journal of physical chemistry. B · 2022Article
- Protein Electrostatics Investigated through Paramagnetic NMR for Nonpolar Groups.The journal of physical chemistry. B · 2022Article
- Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- De novo determination of near-surface electrostatic potentials by NMR.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Quantifying and visualizing weak interactions between anions and proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State.Frontiers in molecular biosciences · 2021Article
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3 authors.
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Abstract
Protein-small cosolute molecule interactions are ubiquitous and known to modulate the solubility, stability, and function of many proteins. Characterization of such transient weak interactions at atomic resolution remains challenging. In this work, we develop a simple and practical NMR method for extracting both energetic and dynamic information on protein-cosolute interactions from solvent paramagnetic relaxation enhancement (sPRE) measurements. Our procedure is based on an approximate (non-Lorentzian) spectral density that behaves exactly at both high and low frequencies. This spectral density contains two parameters, one global related to the translational diffusion coefficient of the paramagnetic cosolute, and the other residue specific. These parameters can be readily determined from sPRE data, and then used to calculate analytically a concentration normalized equilibrium average of the interspin distance, ⟨
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