ArticleMethods in enzymology2019
Characterizing Protein Hydration Dynamics Using Solution NMR Spectroscopy.
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 11 papers.
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11 citing papers in PubMed.
- Improving Protein Structure Determination by Integrating Ensemble-Driven Molecular Dynamics with Chemical Shift-Based Restraints.Journal of chemical information and modeling · 2026Article
- NMR and DFT Studies on Solvation Phenomena in Bioorganic Molecules, Natural Products and Model Compounds: Current and Future Perspectives for Atomic-Level Structures and Mechanistic Catalytic Reactions.Molecules (Basel, Switzerland) · 2026Article
- Visualize Transient Water-Mediated Hydrogen Bonds Facilitating the Formation of Enzymatic Near-Attack Conformers.JACS Au · 2025Article
- Catalytic Serine Labeling in Nonaqueous, Acidic Media.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Characterization of 10MAG/LDAO reverse micelles: Understanding versatility for protein encapsulation.Biophysical chemistry · 2024Article
- Spatial Layouts of Low-Entropy Hydration Shells Guide Protein Binding.Global challenges (Hoboken, NJ) · 2023Article
- Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding.Journal of chemical theory and computation · 2023Article
- The role of NMR in leveraging dynamics and entropy in drug design.Journal 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
- Protein Solvent Shell Structure Provides Rapid Analysis of Hydration Dynamics.Journal of chemical information and modeling · 2019Article
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4 authors.
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Abstract
Protein hydration is a critical aspect of protein stability, folding, and function and yet remains difficult to characterize experimentally. Solution NMR offers a route to a site-resolved view of the dynamics of protein-water interactions through the nuclear Overhauser effects between hydration water and the protein in the laboratory (NOE) and rotating (ROE) frames of reference. However, several artifacts and limitations including contaminating contributions from bulk water potentially plague this general approach and the corruption of measured NOEs and ROEs by hydrogen exchange-relayed magnetization. Fortunately, encapsulation of single protein molecules within the water core of a reverse micelle overcomes these limitations. The main advantages are the suppression hydrogen exchange and elimination of bulk water. Here we detail guidelines for the preparation solutions of encapsulated proteins that are suitable for characterization by NOE and ROE spectroscopy. Emphasis is placed on understanding the contribution of detected NOE intensity arising from magnetization relayed by hydrogen exchange. Various aspects of fitting obtained NOE, selectively decoupled NOE, and ROE time courses are illustrated.
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