T2* weighted Deconvolution of NMR Spectra: Application to 2D Homonuclear MAS Solid-State NMR of Membrane Proteins

V. S. Manu, Tata Gopinath, Songlin Wang, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


2D homonuclear NMR spectroscopy is an essential technique to characterize small and large molecules, such as organic compounds, metabolites, and biomacromolecules at atomic resolution. However, for complex samples 2D homonuclear spectra display poor resolution, making spectral assignment very cumbersome. Here, we propose a new method that exploits the differential T2* relaxation times of individual resonances and resolves the 2D NMR peaks into pseudo-3D spectra, where time is the 3rd dimension. T2* weIghted DEconvolution or TIDE analyzes individual free induction decays (FIDs) and dissects them into sub-FIDs that are transformed into pseudo-3D spectra combining Fourier transformation and covariance NMR. TIDE achieves higher resolution and sensitivity for NMR spectra than classical covariance NMR reducing offset-dependent artifacts. We demonstrate the performance of TIDE for magic angle spinning (MAS) [13C,13C]-DARR NMR spectra of single- and multi-span membrane proteins embedded in lipid bilayers. Since TIDE is applicable to all type of homonuclear correlation experiments for liquid and solid samples, we anticipate that it will be a general method for processing NMR data of biomacromolecules, complex mixtures of metabolites as well as material samples.

Original languageEnglish (US)
Article number8225
JournalScientific reports
Issue number1
StatePublished - Dec 1 2019

Bibliographical note

Funding Information:
This work is supportted by the National Institute of Health (GM 64742 and HL 144130). The authors would like to thank Dr. John Lee and Prof. Hideki Aihara for providing the SatP protein sample. The TIDE software is available from the authors upon request.

Publisher Copyright:
© 2019, The Author(s).


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