Time-resolved multidimensional NMR with non-uniform sampling
Journal of Biomolecular NMR, ISSN: 0925-2738, Vol: 58, Issue: 2, Page: 129-139
2014
- 88Citations
- 109Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations88
- Citation Indexes88
- CrossRef88
- 80
- Captures109
- Readers109
- 109
Article Description
Time-resolved experiments demand high resolution both in spectral dimensions and in time of the studied kinetic process. The latter requirement traditionally prohibits applications of the multidimensional experiments, which, although capable of providing invaluable information about structure and dynamics and almost unlimited spectral resolution, require too lengthy data collection. Our work shows that the problem has a solution in using modern methods of NMR data collection and signal processing. A continuous fast pulsing three-dimensional experiment is acquired using non-uniform sampling during full time of the studied reaction. High sensitivity and time-resolution of a few minutes is achieved by simultaneous processing of the full data set with the multi-dimensional decomposition. The method is verified and illustrated in realistic simulations and by measuring deuterium exchange rates of amide protons in ubiquitin. We applied the method for characterizing kinetics of in vitro phosphorylation of two tyrosine residues in an intrinsically disordered cytosolic domain of the B cell receptor protein CD79b. Signals of many residues including tyrosines in both phosphorylated and unmodified forms of CD79b are found in a heavily crowded region of 2D H-N correlation spectrum and the significantly enhanced spectral resolution provided by the 3D time-resolved approach was essential for the quantitative site-specific analysis. © 2014 The Author(s).
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84896723382&origin=inward; http://dx.doi.org/10.1007/s10858-013-9811-1; http://www.ncbi.nlm.nih.gov/pubmed/24435565; http://link.springer.com/10.1007/s10858-013-9811-1; https://dx.doi.org/10.1007/s10858-013-9811-1; https://link.springer.com/article/10.1007/s10858-013-9811-1
Springer Science and Business Media LLC
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