ArticleJournal of molecular biology2009
Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Encapsulation of Phytochrome Proteins in Trehalose Matrices: Practical Considerations for the Use in Solid-State NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation.Methods in enzymology · 2026Review
- Structural Context Modulates the Conformational Ensemble of the Intrinsically Disordered Amino Terminus of α-Synuclein.Journal of the American Chemical Society · 2025Article
- A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein.Nature communications · 2024Article
- In cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils.bioRxiv : the preprint server for biology · 2024Article
- Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024Review
- Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2023Article
- Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR.Journal of biomolecular NMR · 2022Article
- Time-resolved solid state NMR of biomolecular processes with millisecond time resolution.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Review
- Biomolecular Perturbations in In-Cell Dynamic Nuclear Polarization Experiments.Frontiers in molecular biosciences · 2021Article
- Deuteration of nonexchangeable protons on proteins affects their thermal stability, side-chain dynamics, and hydrophobicity.Protein science : a publication of the Protein Society · 2020Article
- Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020Review
- Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 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
- Disulfide bonds and disorder in granulin-3: An unusual handshake between structural stability and plasticity.Protein science : a publication of the Protein Society · 2017Article
- Low-temperature dynamic nuclear polarization with helium-cooled samples and nitrogen-driven magic-angle spinning.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Article
- The unusual internal motion of the villin headpiece subdomain.Protein science : a publication of the Protein Society · 2016Article
- Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO).Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- NMR at low and ultralow temperatures.Accounts of chemical research · 2013Article
- Dynamic nuclear polarization-enhanced 13C NMR spectroscopy of static biological solids.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
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4 authors.
Funding
Abstract
Solid-state nuclear magnetic resonance (NMR) techniques are used to investigate the structure of the 35-residue villin headpiece subdomain (HP35) in folded, partially denatured, and fully denatured states. Experiments are carried out in frozen glycerol/water solutions, with chemical denaturation by guanidine hydrochloride (GdnHCl). Without GdnHCl, two-dimensional solid-state (13)C NMR spectra of samples prepared with uniform (13)C labeling of selected residues show relatively sharp cross-peaks at chemical shifts that are consistent with the known three-helix bundle structure of folded HP35. At high GdnHCl concentrations, most cross-peaks broaden and shift, qualitatively indicating disruption of the folded structure and development of static conformational disorder in the frozen denatured state. Conformational distributions at one residue in each helical segment are probed quantitatively with three solid-state NMR techniques that provide independent constraints on backbone varphi and psi torsion angles in samples with sequential pairs of carbonyl (13)C labels. Without GdnHCl, the combined data are well fit by alpha-helical conformations. At [GdnHCl]=4.5 M, corresponding to the approximate denaturation midpoint, the combined data are well fit by a combination of alpha-helical and partially extended conformations at each site, but with a site-dependent population ratio. At [GdnHCl]=7.0 M, corresponding to the fully denatured state, the combined data are well fit by a combination of partially extended and polyproline II conformations, again with a site-dependent population ratio. Two entirely different models for conformational distributions lead to nearly the same best-fit distributions, demonstrating the robustness of these conclusions. This work represents the first quantitative investigation of site-specific conformational distributions in partially folded and unfolded states of a protein by solid-state NMR.
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