ArticleProtein science : a publication of the Protein Society2011
The structure of human ubiquitin in 2-methyl-2,4-pentanediol: a new conformational switch.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 50 citations in OpenAlex.
- Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.Journal of the American Chemical Society · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Near atmospheric carbon dioxide activates plant ubiquitin cross-linking.BBA advances · 2023Article
- Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD.Journal of structural biology: X · 2023Article
- A litmus test for classifying recognition mechanisms of transiently binding proteins.Nature communications · 2022Article
- Temperature-Dependent Solid-State NMR Proton Chemical-Shift Values and Hydrogen Bonding.The journal of physical chemistry. B · 2021Article
- Protein Loop Conformational Free Energy Changes via an Alchemical Path without Reaction Coordinates.The journal of physical chemistry letters · 2021Article
- Scaled recoupling of chemical shift anisotropies at high magnetic fields under MAS with interspersed C-elements.The Journal of chemical physics · 2020Article
- Protein conformational dynamics studied bySolid state nuclear magnetic resonance · 2017Article
- Slow conformational exchange and overall rocking motion in ubiquitin protein crystals.Nature communications · 2017Article
- Flexibility and Design: Conformational Heterogeneity along the Evolutionary Trajectory of a Redesigned Ubiquitin.Structure (London, England : 1993) · 2017Article
- Accelerating proton spin diffusion in perdeuterated proteins at 100 kHz MAS.Journal of biomolecular NMR · 2016Article
- Allosteric switch regulates protein-protein binding through collective motion.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Ensembles of a small number of conformations with relative populations.Journal of biomolecular NMR · 2015Article
- Observing the overall rocking motion of a protein in a crystal.Nature communications · 2015Article
- Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.Protein science : a publication of the Protein Society · 2015Article
- Ensemble MD simulations restrained via crystallographic data: accurate structure leads to accurate dynamics.Protein science : a publication of the Protein Society · 2014Article
- Enhancing the quality of protein conformation ensembles with relative populations.Journal of biomolecular NMR · 2014Article
- Motional timescale predictions by molecular dynamics simulations: case study using proline and hydroxyproline sidechain dynamics.Proteins · 2014Article
- Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.Journal of biomolecular NMR · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A new crystal structure of human ubiquitin is reported at 1.8 Å resolution. Compared with the other known crystal structure or the solution NMR structure of monomeric human ubiquitin, this new structure is similar in its overall fold but differs with respect to the conformation of the backbone in a surface-exposed region. The conformation reported here resembles conformations previously seen in complex with deubiquinating enzymes, wherein the Asp52/Gly53 main chain and Glu24 side chain move. This movement exposes the backbone carbonyl of Asp52 to the exterior of the molecule, making it possible to engage in hydrogen-bond contacts with neighboring molecules, rather than in an internal hydrogen bond with the backbone of Glu24. This particular crystal form of ubiquitin has been used in a large number of solid state NMR studies. The structure described here elucidates the origin of many of the chemical shift differences comparing solution and solid state studies.
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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.