ArticleAngewandte Chemie (International ed. in English)2015
Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers.Journal of the American Chemical Society · 2023Article
- Rotating Frame Relaxation in Magic Angle Spinning Solid State NMR, a Promising Tool for Characterizing Biopolymer Motion.Chemical reviews · 2022Review
- Review
- Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR.Nature communications · 2022Article
- Dipolar Order Parameters in Large Systems With Fast Spinning.Frontiers in molecular biosciences · 2021Article
- Model-Free or Not?Frontiers in molecular biosciences · 2021Review
- Experimental Characterization of the Hepatitis B Virus Capsid Dynamics by Solid-State NMR.Frontiers in molecular biosciences · 2021Article
- Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.Biochimica et biophysica acta. Biomembranes · 2020Article
- Relaxation-induced dipolar exchange with recoupling (RIDER) distortions in CODEX experiments.Magnetic resonance (Gottingen, Germany) · 2020Article
- Quantifying Microsecond Exchange in Large Protein Complexes with Accelerated Relaxation Dispersion Experiments in the Solid State.Scientific reports · 2019Article
- Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance RChemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using ComplementaryJournal of the American Chemical Society · 2019Article
- Refocusing CSA during magic angle spinning rotating-frame relaxation experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- Microsecond motions probed by near-rotary-resonance RJournal of biomolecular NMR · 2018Article
- Protein conformational dynamics studied bySolid state nuclear magnetic resonance · 2017Article
- Characterization of Protein-Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements.Journal of the American Chemical Society · 2017Article
- Slow conformational exchange and overall rocking motion in ubiquitin protein crystals.Nature communications · 2017Article
- Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein.Journal of the American Chemical Society · 2017Article
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Authors and funding
4 authors.
Funding
Abstract
Understanding the dynamics of interacting proteins is a crucial step toward describing many biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two different assemblies: crystalline GB1 and the precipitated GB1-antibody complex with a molecular weight of more than 300 kDa. We perform these measurements on samples containing as little as eight nanomoles of GB1. From measurements of site-specific (15) N relaxation rates including relaxation dispersion we obtain snapshots of dynamics spanning nine orders of magnitude in terms of the time scale. A comparison of measurements for GB1 in either environment reveals that while many of the dynamic features of the protein are conserved between them (in particular for the fast picosecond-nanosecond motions), much greater differences occur for slow motions with motions in the >500 ns range being more prevalent in the complex. The data suggest that GB1 can potentially undergo a small-amplitude overall anisotropic motion sampling the interaction interface in the complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.