ArticleJournal of the American Chemical Society2011
Mapping the hydration dynamics of ubiquitin.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 108 citations in OpenAlex.
- Hydration Contribution to the Solvation Free Energy of Water-Soluble Polymers.The journal of physical chemistry. B · 2025Article
- Advances in utilizing reverse micelles to investigate membrane proteins.Biochemical Society transactions · 2024Review
- Characterization of 10MAG/LDAO reverse micelles: Understanding versatility for protein encapsulation.Biophysical chemistry · 2024Article
- NMR Dynamic View of the Destabilization of WW4 Domain by Chaotropic GdmCl and NaSCN.International journal of molecular sciences · 2024Article
- Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding.Journal of chemical theory and computation · 2023Article
- Deep mining of the protein energy landscape.Structural dynamics (Melville, N.Y.) · 2023Article
- Confinement dependence of protein-associated solvent dynamics around different classes of proteins, from the EPR spin probe perspective.Physical chemistry chemical physics : PCCP · 2022Article
- Universal dynamical onset in water at distinct material interfaces.Chemical science · 2022Article
- Resolution and characterization of confinement- and temperature-dependent dynamics in solvent phases that surround proteins in frozen aqueous solution by using spin-probe EPR spectroscopy.Methods in enzymology · 2022Article
- THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY-MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- Development of effective potassium acetate extractant.RSC advances · 2021Article
- Protein conformational entropy is not slaved to water.Scientific reports · 2020Article
- Mechanical Unfolding of Spectrin Repeats Induces Water-Molecule Ordering.Biophysical journal · 2020Article
- Article
- Site-Resolved and Quantitative Characterization of Very Weak Protein-Ligand Interactions.ACS chemical biology · 2019Article
- Protein Solvent Shell Structure Provides Rapid Analysis of Hydration Dynamics.Journal of chemical information and modeling · 2019Article
- Characterizing Protein Hydration Dynamics Using Solution NMR Spectroscopy.Methods in enzymology · 2019Article
- Reverse Micelle Encapsulation of Proteins for NMR Spectroscopy.Methods in enzymology · 2019Article
- Water-Protein Interactions Coupled with Protein Conformational Transition.Biophysical journal · 2018Article
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nature of water's interaction with biomolecules such as proteins has been difficult to examine in detail at atomic resolution. Solution NMR spectroscopy is potentially a powerful method for characterizing both the structural and temporal aspects of protein hydration but has been plagued by artifacts. Encapsulation of the protein of interest within the aqueous core of a reverse micelle particle results in a general slowing of water dynamics, significant reduction in hydrogen exchange chemistry and elimination of contributions from bulk water thereby enabling the use of nuclear Overhauser effects to quantify interactions between the protein surface and hydration water. Here we extend this approach to allow use of dipolar interactions between hydration water and hydrogens bonded to protein carbon atoms. By manipulating the molecular reorientation time of the reverse micelle particle through use of low viscosity liquid propane, the T(1ρ) relaxation time constants of (1)H bonded to (13)C were sufficiently lengthened to allow high quality rotating frame nuclear Overhauser effects to be obtained. These data supplement previous results obtained from dipolar interactions between the protein and hydrogens bonded to nitrogen and in aggregate cover the majority of the molecular surface of the protein. A wide range of hydration dynamics is observed. Clustering of hydration dynamics on the molecular surface is also seen. Regions of long-lived hydration water correspond with regions of the protein that participate in molecular recognition of binding partners suggesting that the contribution of the solvent entropy to the entropy of binding has been maximized through evolution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.