ArticleAngewandte Chemie (International ed. in English)2019
Localized and Collective Motions in HET-s(218-289) Fibrils from Combined NMR Relaxation and MD Simulation.
Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 33 citations in OpenAlex.
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- Probing the Dynamics of Yersinia Adhesin A (YadA) in Outer Membranes Hints at Requirements for β-Barrel Membrane Insertion.Journal of the American Chemical Society · 2025Article
- Analytical Framework to Understand the Origins of Methyl Side-Chain Dynamics in Protein Assemblies.Journal of the American Chemical Society · 2024Article
- New experimental evidence for pervasive dynamics in proteins.Protein science : a publication of the Protein Society · 2023Article
- Review
- A method to construct the dynamic landscape of a bio-membrane with experiment and simulation.Nature communications · 2022Article
- Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR.Chemical science · 2021Review
- How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?Journal of biomolecular NMR · 2021Article
- Experimental Characterization of the Hepatitis B Virus Capsid Dynamics by Solid-State NMR.Frontiers in molecular biosciences · 2021Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Model-Free or Not?Frontiers in molecular biosciences · 2021Review
- Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Review
- Localized and Collective Motions in HET-s(218-289) Fibrils from Combined NMR Relaxation and MD Simulation.Angewandte Chemie (International ed. in English) · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Nuclear magnetic resonance (NMR) relaxation data and molecular dynamics (MD) simulations are combined to characterize the dynamics of the fungal prion HET-s(218-289) in its amyloid form. NMR data is analyzed with the dynamics detector method, which yields timescale-specific information. An analogous analysis is performed on MD trajectories. Because specific MD predictions can be verified as agreeing with the NMR data, MD was used for further interpretation of NMR results: for the different timescales, cross-correlation coefficients were derived to quantify the correlation of the motion between different residues. Short timescales are the result of very local motions, while longer timescales are found for longer-range correlated motion. Similar trends on ns- and μs-timescales suggest that μs motion in fibrils is the result of motion correlated over many fibril layers.
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