ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2007
Changes in protein structure and dynamics as a function of hydration from (1)H second moments.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
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- Primary biomolecular adsorption energetics of core-shell nanocomplexes: Implications for biological interactions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Distribution of Gadolinium in Rat Heart Studied by Fast Field Cycling Relaxometry and Imaging SIMS.International journal of molecular sciences · 2019Article
- NMR chemical shift pattern changed by ammonium sulfate precipitation in cyanobacterial phytochrome Cph1.Frontiers in molecular biosciences · 2015Article
- Temperature dependence of lysozyme hydration and the role of elastic energy.Physical review. E, Statistical, nonlinear, and soft matter physics · 2011Article
- Water and backbone dynamics in a hydrated protein.Biophysical journal · 2010Article
- Global and local mobility of apocalmodulin monitored through fast-field cycling relaxometry.Biophysical journal · 2009Article
- Water molecule contributions to proton spin-lattice relaxation in rotationally immobilized proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- Hydrogen skeleton, mobility and protein architecture.Intrinsically disordered proteinsArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
We report the proton second moment obtained directly from the Free Induction Decay (FID) of the NMR signal of variously hydrated bovine serum albumin (BSA) and hen egg white lysozyme (HEWL) and from the width of the NMR Z-spectrum of the cross-linked protein gels of different concentrations. The second moment of the proteins decreases in a continuous stepwise way as a function of increasing water content, which suggests that the structural and dynamical changes occur in small incremental steps. Although the second moment is dominated by the short range distances of nearest neighbors, the changes in the second moment show that the protein structure becomes more open with increasing hydration level. A difference between the apparent liquid content of the sample as found from decomposition of the FID and the analytically determined water content demonstrates that water absorbed in the early stages of hydration is motionally immobilized and magnetically indistinguishable from rigid protein protons while at high hydration levels some protein side-chain protons move rapidly contributing to liquid-like component of the NMR signal.
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Registered trials
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