ArticleJournal of biomolecular NMR2013
Internal protein dynamics on ps to μs timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Review
- Model-Free or Not?Frontiers in molecular biosciences · 2021Review
- Relaxing with liquids and solids - A perspective on biomolecular dynamics.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Review
- Quantifying Microsecond Exchange in Large Protein Complexes with Accelerated Relaxation Dispersion Experiments in the Solid State.Scientific reports · 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
- Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR.Chemphyschem : 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
- Microsecond motions probed by near-rotary-resonance RJournal of biomolecular NMR · 2018Article
- Protein conformational dynamics studied bySolid state nuclear magnetic resonance · 2017Article
- Slow conformational exchange and overall rocking motion in ubiquitin protein crystals.Nature communications · 2017Article
- Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein.Journal of the American Chemical Society · 2017Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.Progress in nuclear magnetic resonance spectroscopy · 2016Review
- Characterization of fibril dynamics on three timescales by solid-state NMR.Journal of biomolecular NMR · 2016Article
- Sequential backbone assignment based on dipolar amide-to-amide correlation experiments.Journal of biomolecular NMR · 2015Article
- Integrative, dynamic structural biology at atomic resolution--it's about time.Nature methods · 2015Review
- NMR studies of dynamic biomolecular conformational ensembles.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins.Journal of biomolecular NMR · 2014Article
- Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes.Journal of biomolecular NMR · 2014Article
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5 authors.
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Abstract
A comprehensive analysis of the dynamics of the SH3 domain of chicken alpha-spectrin is presented, based upon (15)N T1 and on- and off-resonance T1ρ relaxation times obtained on deuterated samples with a partial back-exchange of labile protons under a variety of the experimental conditions, taking explicitly into account the dipolar order parameters calculated from (15)N-(1)H dipole-dipole couplings. It is demonstrated that such a multi-frequency approach enables access to motional correlation times spanning about 6 orders of magnitude. We asses the validity of different motional models based upon orientation autocorrelation functions with a different number of motional components. We find that for many residues a "two components" model is not sufficient for a good description of the data and more complicated fitting models must be considered. We show that slow motions with correlation times on the order of 1-10 μs can be determined reliably in spite of rather low apparent amplitudes (below 1 %), and demonstrate that the distribution of the protein backbone mobility along the time scale axis is pronouncedly non-uniform and non-monotonic: two domains of fast (τ < 10(-10) s) and intermediate (10(-9) s < τ < 10(-7) s) motions are separated by a gap of one order of magnitude in time with almost no motions. For slower motions (τ > 10(-6) s) we observe a sharp ~1 order of magnitude decrease of the apparent motional amplitudes. Such a distribution obviously reflects different nature of backbone motions on different time scales, where the slow end may be attributed to weakly populated "excited states." Surprisingly, our data reveal no clearly evident correlations between secondary structure of the protein and motional parameters. We also could not notice any unambiguous correlations between motions in different time scales along the protein backbone emphasizing the importance of the inter-residue interactions and the cooperative nature of protein dynamics.
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