ReviewMethods in enzymology2026
Dynamics studies of side-chains and hydration shells in amyloid-β fibrils using deuterium and oxygen-17 solid-state NMR.
Review in Methods in enzymology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Hydration water dynamics in amyloid-β aggregates using deuterium and oxygen-17 solid-state NMR spectroscopy.The Journal of chemical physics · 2026Article
- Article
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Abstract
This review focuses on deuterium and oxygen-17 solid-state NMR methods for studies of dynamics in amyloid-beta fibrils in rehydrated lyophilized states. For both nuclei NMR spectroscopic properties are dominated by the quadrupolar interaction. Deuterium NMR methods for studies of side-chain dynamics cover line shape analysis, longitudinal Zeeman and Quadrupolar order relaxation, transverse relaxation using Qudrupolar Carr Purcell Meiboom Gill scheme real-time detection, rotating frame relaxation (including off-resonance and quadrupolar order locking), and Chemical Exchange Saturation Transfer methods. Examples are chosen based on the results obtained for native and post-translationally modified fibrils under static and magic-angle spinning conditions. Oxygen-17 laboratory and rotating frame relaxation methods focusing on detection of the central transition under static conditions are presented for hydration shell dynamics in pyroglutateme-3 modified fibrils. Experimental methodology is supplemented with description of explicit motional modeling approaches to arrive at quantitative description of dynamical modes and their corresponding parameters. Special emphasis is placed on the complementarity of different approaches to obtain a fuller picture of motions.
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