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Updated: May 6, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Sensitivity and resolution enhancement of oriented solid-state NMR: application to membrane proteins

T Gopinath1, Kaustubh R Mote, Gianluigi Veglia

  • 1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, United States.

Progress in Nuclear Magnetic Resonance Spectroscopy
|October 29, 2013
PubMed
Summary

Oriented solid-state NMR (O-ssNMR) spectroscopy enables detailed analysis of transmembrane proteins. Optimized pulse sequences using lipid bicelles improve spectral resolution and sensitivity for structural determination.

Keywords:
4-pentyl-4′-cyanobiphenyl5CBBLEWBurum Linser Ernst WindowlessCPCSAChemical shift anisotropyDCDTRFDipolar couplingsFSLGFrequency-Switched Lee-GoldbergHETCORHIMSELFHeteronuclear Isotropic Mixing Separated Local FieldLGLee-GoldbergMASMLEVMSHOTMagic Sandwich Higher Order TruncationMalcolm Levitt Decoupling SequenceN-acetyl-leucineN-acetyl-valine-leucineNALNAVLO-ssNMROriented solid-state NMRPDSDPELFPIPISEMAPLNProton Evolved Local FieldRMSResolution enhancementSAMPI4SESLNSNRSarcolipinSelective Averaging Magic Sandwich with Polarization InversionSensitivity enhancementWIM24Windowless Isotropic Mixing 24chemical shift anisotropycross polarizationdipolar couplingdoubly tilted rotating frameheteronuclear correlationmagic angle spinningoriented solid-state NMRphospholambanpolarization inversionpolarization inversion spin exchange at the magic angleproton driven spin diffusionroot mean squaresensitivity enhancementsignal to noise ratio

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