ArticleJournal of biomolecular NMR2011
Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- NMRlib: user-friendly pulse sequence tools for Bruker NMR spectrometers.Journal of biomolecular NMR · 2019Article
- An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function.Science advances · 2018Article
- Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.Cell · 2015Article
- Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.PLoS pathogens · 2013Article
- An improved algorithm for MFR fragment assembly.Journal of biomolecular NMR · 2012Article
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been demonstrated that protein folds can be determined using appropriate computational protocols with NMR chemical shifts as the sole source of experimental restraints. While such approaches are very promising they still suffer from low convergence resulting in long computation times to achieve accurate results. Here we present a suite of time- and sensitivity optimized NMR experiments for rapid measurement of up to six RDCs per residue. Including such an RDC data set, measured in less than 24 h on a single aligned protein sample, greatly improves convergence of the Rosetta-NMR protocol, allowing for overnight fold calculation of small proteins. We demonstrate the performance of our fast fold calculation approach for ubiquitin as a test case, and for two RNA-binding domains of the plant protein HYL1. Structure calculations based on simulated RDC data highlight the importance of an accurate and precise set of several complementary RDCs as additional input restraints for high-quality de novo structure determination.
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