ArticleThe journal of physical chemistry. B2013
Glassy dynamics of protein methyl groups revealed by deuteron NMR.
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Dynamics studies of side-chains and hydration shells in amyloid-β fibrils using deuterium and oxygen-17 solid-state NMR.Methods in enzymology · 2026Review
- Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024Article
- The contribution of methyl groups to electron spin decoherence of nitroxides in glassy matrices.The Journal of chemical physics · 2024Article
- Effect of Cross-Seeding of Wild-Type Amyloid-βThe journal of physical chemistry. B · 2023Article
- Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.Solid state nuclear magnetic resonance · 2021Review
- Deuteration of nonexchangeable protons on proteins affects their thermal stability, side-chain dynamics, and hydrophobicity.Protein science : a publication of the Protein Society · 2020Article
- Dynamics of Serine-8 Side-Chain in Amyloid-β Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR.The journal of physical chemistry. B · 2020Article
- Influenza A M2 Channel Clustering at High Protein/Lipid Ratios: Viral Budding Implications.Biophysical journal · 2019Article
- Basic experiments inMethods (San Diego, Calif.) · 2018Review
- Static solid-stateProgress in nuclear magnetic resonance spectroscopy · 2017Review
- Solid state deuterium NMR study of LKα14 peptide aggregation in biosilica.Biointerphases · 2017Article
- Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.The journal of physical chemistry. B · 2017Article
- Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils.Chemical physics letters · 2017Article
- Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.Biophysical journal · 2016Article
- Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR.The journal of physical chemistry. B · 2015Article
- (15)N CSA tensors and (15)N-(1)H dipolar couplings of protein hydrophobic core residues investigated by static solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Protein dynamics in the solid state from 2H NMR line shape analysis: a consistent perspective.The journal of physical chemistry. B · 2015Article
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5 authors.
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Abstract
We investigated site-specific dynamics of key methyl groups in the hydrophobic core of chicken villin headpiece subdomain (HP36) over the temperature range between 298 and 140 K using deuteron solid-state NMR longitudinal relaxation measurements. The relaxation of the longitudinal magnetization is weakly nonexponential (glassy) at high temperatures and exhibits a stronger degree of nonexponentiality below about 175 K. In addition, the characteristic relaxation times deviate from the simple Arrhenius law. We interpret this behavior via the existence of distribution of activation energy barriers for the three-site methyl jumps, which originates from somewhat different methyl environments within the local energy landscape. The width of the distribution of the activation barriers for methyl jumps is rather significant, about 1.4 kJ/mol. Our experimental results and modeling allow for the description of the apparent change at about 175 K without invoking a specific transition temperature. For most residues in the core, the relaxation behavior at high temperatures points to the existence of conformational exchange between the substates of the landscape, and our model takes into account the kinetics of this process. The observed dynamics are the same for dry and hydrated protein. We also looked at the effect of F58L mutation inside the hydrophobic core on the dynamics of one of the residues and observed a significant increase in its conformational exchange rate constant at high temperatures.
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