ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2009
Water molecule contributions to proton spin-lattice relaxation in rotationally immobilized proteins.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 35 citations in OpenAlex.
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- Understanding water properties in tumorous murine cells using field-cycling NMR relaxometry.Scientific reports · 2025Article
- Markers of low field NMR relaxation features of tissues.Scientific reports · 2024Article
- Water Dynamics in Highly Concentrated Protein Systems-Insight from Nuclear Magnetic Resonance Relaxometry.International journal of molecular sciences · 2023Article
- Stability of the Meat Protein Type I Collagen: Influence of pH, Ionic Strength, and Phenolic Antioxidant.Foods (Basel, Switzerland) · 2020Article
- Article
- Distribution of Gadolinium in Rat Heart Studied by Fast Field Cycling Relaxometry and Imaging SIMS.International journal of molecular sciences · 2019Article
- Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein.Protein science : a publication of the Protein Society · 2014Article
- Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.Journal of biomolecular NMR · 2013Article
- Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Spin-lattice relaxation rates of protein and water protons in dry and hydrated immobilized bovine serum albumin were measured in the range of (1)H Larmor frequency from 10 kHz to 30 MHz at temperatures from 154 to 302 K. The water proton spin-lattice relaxation reports on that of protein protons, which causes the characteristic power law dependence on the magnetic field strength. Isotope substitution of deuterium for hydrogen in water and studies at different temperatures expose three classes of water molecule dynamics that contribute to the spin-lattice relaxation dispersion profile. At 185 K, a water (1)H relaxation contribution derives from reorientation of protein-bound molecules that are dynamically uncoupled from the protein backbone and is characterized by a Lorentzian function. Bound-water-molecule motions that can be dynamically uncoupled or coupled to the protein fluctuations make dominant contributions at higher temperatures as well. Surface water translational diffusion that is magnetically two-dimensional makes relaxation contributions at frequencies above 10 MHz. It is shown using isotope substitution that the exponent of the power law of the water signal in hydrated immobilized protein systems is the same as that for protons in lyophilized proteins over four orders of magnitude in the Larmor frequency, which implies that changes in the protein structure associated with hydration do not affect the (1)H spin relaxation.
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