ArticleJournal of the American Chemical Society2016
Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D ²H-¹³C-¹³C Solid-State NMR Spectroscopy.
Article in Journal of the American Chemical Society, 2016. 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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31 citing papers in PubMed, 55 citations in OpenAlex.
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- Probe design for high sensitivity proton-detected solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024Article
- Carbon-detected deuterium solid-state NMR rotating frame relaxation measurements for protein methyl groups under magic angle spinning.Solid state nuclear magnetic resonance · 2024Article
- Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024Article
- 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
- Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR.Magnetic resonance (Gottingen, Germany) · 2024Article
- Deuteron off-resonance rotating frame relaxation for the characterization of slow motions in rotating and static solid-state proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Structural and dynamical investigation of histone H2B in well-hydrated nucleosome core particles by solid-state NMR.Communications biology · 2023Article
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- Assignment of aromatic side-chain spins and characterization of their distance restraints at fast MAS.Journal of structural biology: X · 2023Article
- Solid-State NMRThe journal of physical chemistry. A · 2022Article
- Beyond structure: Deciphering site-specific dynamics in proteins from double histidine-based EPR measurements.Protein science : a publication of the Protein Society · 2022Article
- Article
- Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3DJournal of biomolecular NMR · 2022Article
- Recent Advances in Investigating Functional Dynamics of Chromatin.Frontiers in genetics · 2022Review
- Off-resonanceJournal of biomolecular NMR · 2021Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Dynamic networks observed in the nucleosome core particles couple the histone globular domains with DNA.Communications biology · 2020Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
(2)H quadrupolar line shapes deliver rich information about protein dynamics. A newly designed 3D (2)H-(13)C-(13)C solid-state NMR magic angle spinning (MAS) experiment is presented and demonstrated on the microcrystalline β1 immunoglobulin binding domain of protein G (GB1). The implementation of (2)H-(13)C adiabatic rotor-echo-short-pulse-irradiation cross-polarization (RESPIRATION CP) ensures the accuracy of the extracted line shapes and provides enhanced sensitivity relative to conventional CP methods. The 3D (2)H-(13)C-(13)C spectrum reveals (2)H line shapes for 140 resolved aliphatic deuterium sites. Motional-averaged (2)H quadrupolar parameters obtained from the line-shape fitting identify side-chain motions. Restricted side-chain dynamics are observed for a number of polar residues including K13, D22, E27, K31, D36, N37, D46, D47, K50, and E56, which we attribute to the effects of salt bridges and hydrogen bonds. In contrast, we observe significantly enhanced side-chain flexibility for Q2, K4, K10, E15, E19, N35, N40, and E42, due to solvent exposure and low packing density. T11, T16, and T17 side chains exhibit motions with larger amplitudes than other Thr residues due to solvent interactions. The side chains of L5, V54, and V29 are highly rigid because they are packed in the core of the protein. High correlations were demonstrated between GB1 side-chain dynamics and its biological function. Large-amplitude side-chain motions are observed for regions contacting and interacting with immunoglobulin G (IgG). In contrast, rigid side chains are primarily found for residues in the structural core of the protein that are absent from protein binding and interactions.
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