ArticleJournal of the American Chemical Society2012
Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.Nature chemistry · 2026Article
- Dynamics of hydrogen-bonded end groups in bulk polymers revealed by solid-state NMR spectroscopy relaxation dispersion experiments.Communications chemistry · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- DHFR Mutants Modulate Their Synchronized Dynamics with the Substrate by Shifting Hydrogen Bond Occupancies.Journal of chemical information and modeling · 2022Article
- Review
- Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.Solid state nuclear magnetic resonance · 2021Review
- Experimental Characterization of the Hepatitis B Virus Capsid Dynamics by Solid-State NMR.Frontiers in molecular biosciences · 2021Article
- Paramagnetic relaxation enhancement-assisted structural characterization of a partially disordered conformation of ubiquitin.Protein science : a publication of the Protein Society · 2019Article
- Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N Terminus.Biophysical journal · 2019Article
- Relaxing with liquids and solids - A perspective on biomolecular dynamics.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Review
- Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by SpecificJournal of the American Chemical Society · 2019Article
- Deuteron Solid-State NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N-Terminal Domain of Amyloid-β Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies.The journal of physical chemistry. B · 2019Article
- Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency.Journal of structural biology · 2019Article
- Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance RChemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using ComplementaryJournal of the American Chemical Society · 2019Article
- Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.Nature communications · 2018Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Protein conformational dynamics studied bySolid state nuclear magnetic resonance · 2017Article
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Authors and funding
5 authors.
Funding
Abstract
We demonstrate that conformational exchange processes in proteins on microsecond-to-millisecond time scales can be detected and quantified by solid-state NMR spectroscopy. We show two independent approaches that measure the effect of conformational exchange on transverse relaxation parameters, namely Carr-Purcell-Meiboom-Gill relaxation-dispersion experiments and measurement of differential multiple-quantum coherence decay. Long coherence lifetimes, as required for these experiments, are achieved by the use of highly deuterated samples and fast magic-angle spinning. The usefulness of the approaches is demonstrated by application to microcrystalline ubiquitin. We detect a conformational exchange process in a region of the protein for which dynamics have also been observed in solution. Interestingly, quantitative analysis of the data reveals that the exchange process is more than 1 order of magnitude slower than in solution, and this points to the impact of the crystalline environment on free energy barriers.
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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.