ArticleThe journal of physical chemistry. B2009
Dimensionality of diffusive exploration at the protein interface in solution.
Article in The journal of physical chemistry. B, 2009. 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, 51 citations in OpenAlex.
- Direct evidence of acid-driven protein desolvation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Understanding water properties in tumorous murine cells using field-cycling NMR relaxometry.Scientific reports · 2025Article
- Impact of water models on the structure and dynamics of enzyme tunnels.Computational and structural biotechnology journal · 2024Article
- Markers of low field NMR relaxation features of tissues.Scientific reports · 2024Article
- Diffusion of Water Molecules on the Surface of Silica Nanoparticles─Insights from Nuclear Magnetic Resonance Relaxometry.The journal of physical chemistry. B · 2024Article
- Water Dynamics in Highly Concentrated Protein Systems-Insight from Nuclear Magnetic Resonance Relaxometry.International journal of molecular sciences · 2023Article
- Ion influence on surface water dynamics and proton exchange at protein surfaces - A unified model for transverse and longitudinal NMR relaxation dispersion.Journal of molecular liquids · 2022Article
- Seeking Solvation: Exploring the Role of Protein Hydration in Silk Gelation.Molecules (Basel, Switzerland) · 2022Article
- Ion-specificity and surface water dynamics in protein solutions.Physical chemistry chemical physics : PCCP · 2018Article
- Single-file transport of water through membrane channels.Faraday discussions · 2018Article
- Water Dynamics in the Hydration Shells of Biomolecules.Chemical reviews · 2017Review
- Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.The Journal of biological chemistry · 2016Article
- Water Determines the Structure and Dynamics of Proteins.Chemical reviews · 2016Review
- The Clusters-in-a-Liquid Approach for Solvation: New Insights from the Conformer Specific Gas Phase Spectroscopy and Vibrational Optical Activity Spectroscopy.Frontiers in chemistry · 2016Review
- Water dynamics in protein hydration shells: the molecular origins of the dynamical perturbation.The journal of physical chemistry. B · 2014Article
- Direct probing of solvent accessibility and mobility at the binding interface of polymerase (Dpo4)-DNA complex.The journal of physical chemistry. A · 2013Article
- The magnetic field dependence of water T1 in tissues.Magnetic resonance in medicine · 2012Article
- Water-proton-spin-lattice-relaxation dispersion of paramagnetic protein solutions.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- Water and backbone dynamics in a hydrated protein.Biophysical journal · 2010Article
- Water molecule contributions to proton spin-lattice relaxation in rotationally immobilized proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The dynamics of water are critically important to the energies of interaction between proteins and substrates and determine the efficiency of transport at the interface. The magnetic field dependence of the nuclear spin-lattice relaxation rate constant 1/T(1) of water protons provides a direct characterization of water diffusional dynamics at the protein interface. We find that the surface-average translational correlation time is 30-40 ps and the magnetic field dependence of the water proton 1/T(1) is characteristic of two-dimensional diffusion of water in the protein interfacial region. The reduced dimensionality substantially increases the intermolecular re-encounter probability and the efficiency of the surface exploration by the small molecule, water in this case. We propose a comprehensive theory of the translational effects of a small diffusing particle confined in the vicinity of a spherical macromolecule as a function of the relative size of the two particles. We show that the change in the apparent dimensionality of the diffusive exploration is a general result of the small diffusing particle encountering a much larger particle that presents a diffusion barrier. Examination of the effects of the size of the confinement relative to the macromolecule size reveals that the reduced dimensionality characterizing the small-molecule diffusion persists to remarkably small radius ratios. The experimental results on several different proteins in solution support the proposed theoretical model, which may be generalized to other small-particle-large-body systems like vesicles and micelles.
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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.