ArticleProtein science : a publication of the Protein Society2019
Paramagnetic relaxation enhancement-assisted structural characterization of a partially disordered conformation of ubiquitin.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Characterizing conformational ensembles of multi-domain proteins using anisotropic paramagnetic NMR restraints.Biophysical reviews · 2022Review
- Nonthermal excitation effects mediated by sub-terahertz radiation on hydrogen exchange in ubiquitin.Biophysical journal · 2021Article
- Paramagnetic relaxation enhancement-assisted structural characterization of a partially disordered conformation of ubiquitin.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
6 authors.
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Abstract
Nuclear magnetic resonance (NMR) is a powerful tool to study three-dimensional structures as well as protein conformational fluctuations in solution, but it is compromised by increases in peak widths and missing signals. We previously reported that ubiquitin has two folded conformations, N
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Registered trials
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