ArticleBiochemistry2011
Slow motions in the hydrophobic core of chicken villin headpiece subdomain and their contributions to configurational entropy and heat capacity from solid-state deuteron NMR measurements.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 43 citations in OpenAlex.
- Dynamics studies of side-chains and hydration shells in amyloid-β fibrils using deuterium and oxygen-17 solid-state NMR.Methods in enzymology · 2026Review
- Multi-mode water dynamics in hydration shells of villin headpiece subdomain protein in the solid state using deuterium and oxygen-17 NMR spectroscopy.The Journal of chemical physics · 2025Article
- Temperature-Dependent Rotation of Protonated Methyl Groups in Otherwise Deuterated Proteins Modulates DEER Distance Distributions.Applied magnetic resonance · 2025Article
- Persistence of Methionine Side Chain Mobility at Low Temperatures in a Nine-Residue Low Complexity Peptide, as Probed byChemphyschem : a European journal of chemical physics and physical chemistry · 2024Article
- Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles.Physical chemistry chemical physics : PCCP · 2024Article
- Effect of Cross-Seeding of Wild-Type Amyloid-βThe journal of physical chemistry. B · 2023Article
- Comparative Hydrophobic Core Dynamics Between Wild-Type Amyloid-β Fibrils, Glutamate-3 Truncation, and Serine-8 Phosphorylation.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022Article
- Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-β fibrils.Magnetic resonance in chemistry : MRC · 2021Article
- 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
- Deuteron Quadrupolar Chemical Exchange Saturation Transfer (Q-CEST) Solid-State NMR for Static Powder Samples: Approach and Applications to Amyloid-β Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Local ordering and dynamics in anisotropic media by magnetic resonance: from liquid crystals to proteins.Liquid crystals · 2020Article
- Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils.The Journal of biological chemistry · 2019Article
- Protein dynamics in the solid-state fromSolid state nuclear magnetic resonance · 2018Article
- 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
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
We have investigated microsecond to millisecond time scale dynamics in several key hydrophobic core methyl groups of chicken villin headpiece subdomain protein (HP36) using a combination of single-site labeling, deuteron solid-state NMR line shape analysis, and computational modeling. Deuteron line shapes of hydrated powder samples are dominated by rotameric jumps and show a large variability of rate constants, activation energies, and rotameric populations. Site-specific activation energies vary from 6 to 38 kJ/mol. An additional mode of diffusion on a restricted arc is significant for some sites. In dry samples, the dynamics is quenched. Parameters of the motional models allow for calculations of configurational entropy and heat capacity, which, together with the rate constants, allow for observation of interplay between thermodynamic and kinetic picture of the landscape. Mutations at key phenylalanine residues at both distal (F47L&F51L) and proximal (F58L) locations to a relatively rigid side chain of L69 have a pronounced effect on alleviating the rigidity of this side chain at room temperature and demonstrate the sensitivity of the hydrophobic core environment to such perturbations.
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