ArticleJournal of the American Chemical Society2010
Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed.
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- Insights into Molecular Diversity within the FET Family: Unraveling Phase Separation of the N-Terminal Low Complexity Domain from RNA-Binding Protein EWS.bioRxiv : the preprint server for biology · 2023Article
- Intracellular environment can change protein conformational dynamics in cells through weak interactions.Science advances · 2023Article
- Bromodomain Interactions with Acetylated Histone 4 Peptides in the BRD4 Tandem Domain: Effects on Domain Dynamics and Internal Flexibility.Biochemistry · 2022Article
- Extensive tests and evaluation of the CHARMM36IDPSFF force field for intrinsically disordered proteins and folded proteins.Physical chemistry chemical physics : PCCP · 2019Article
- NMR Methods for Characterizing the Basic Side Chains of Proteins: Electrostatic Interactions, Hydrogen Bonds, and Conformational Dynamics.Methods in enzymology · 2019Review
- What DrivesBiophysical journal · 2018Article
- Correlated motions of C'-N and CJournal of biomolecular NMR · 2018Article
- Fast evaluation of protein dynamics from deficientJournal of biomolecular NMR · 2018Article
- Quantifying protein dynamics in the ps-ns time regime by NMR relaxation.Journal of biomolecular NMR · 2016Article
- Article
- (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
- NMR studies of dynamic biomolecular conformational ensembles.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Time-shared experiments for efficient assignment of triple-selectively labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Biophysical journal · 2014Article
- Spectral density mapping protocols for analysis of molecular motions in disordered proteins.Journal of biomolecular NMR · 2014Article
- A 13C labeling strategy reveals a range of aromatic side chain motion in calmodulin.Journal of the American Chemical Society · 2013Article
- The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics.Biopolymers · 2013Review
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Abstract
Site-specific (15)N chemical shift anisotropy (CSA) tensors have been derived for the well-ordered backbone amide (15)N nuclei in the B3 domain of protein G (GB3) from residual chemical shift anisotropy (RCSA) measured in six different mutants that retain the native structure but align differently relative to the static magnetic field when dissolved in a liquid crystalline Pf1 suspension. This information is complemented by measurement of cross-correlated relaxation rates between the (15)N CSA tensor and either the (15)N-(1)H or (15)N-(13)C' dipolar interaction. In agreement with recent solid state NMR measurements, the (15)N CSA tensors exhibit only a moderate degree of variation from averaged values, but have larger magnitudes in alpha-helical (-173 +/- 7 ppm) than in beta-sheet (-162 +/- 6 ppm) residues, a finding also confirmed by quantum computations. The orientations of the least shielded tensor component cluster tightly around an in-peptide-plane vector that makes an angle of 19.6 +/- 2.5 degrees with the N-H bond, with the asymmetry of the (15)N CSA tensor being slightly smaller in alpha-helix (eta = 0.23 +/- 0.17) than in beta-sheet (eta = 0.31 +/- 0.11). The residue-specific (15)N CSA values are validated by improved agreement between computed and experimental (15)N R(1rho) relaxation rates measured for (15)N-{(2)H} sites in GB3, which are dominated by the CSA mechanism. Use of residue-specific (15)N CSA values also results in more uniform generalized order parameters, S(2), and predicts considerable residue-by-residue variations in the magnetic field strengths where TROSY line narrowing is most effective.
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