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Related Experiment Videos

Adiabatic TOBSY in rotating solids.

Jörg Leppert1, Oliver Ohlenschläger, Matthias Görlach

  • 1Abteilung Molekulare Biophysik/NMR-Spektroskopie, Institut für Molekulare Biotechnologie, 07745 Jena, Germany.

Journal of Biomolecular NMR
|March 12, 2004
PubMed
Summary

This study introduces a new solid-state Nuclear Magnetic Resonance (NMR) method for analyzing peptides and proteins. The technique efficiently maps through-bond carbon-13 (¹³C) chemical shift correlations in aliphatic regions.

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Structural Biology
  • Biophysics

Background:

  • Solid-state NMR is crucial for determining the structure of biomolecules that are difficult to crystallize.
  • Efficiently correlating chemical shifts through-bonds in solid-state NMR is essential for structural elucidation.
  • Existing methods may have limitations in speed or applicability to uniformly labeled samples.

Purpose of the Study:

  • To develop a novel Magnetic Angle Spinning (MAS) solid-state NMR approach for efficient through-bond ¹³C chemical shift correlations.
  • To enable detailed structural analysis of aliphatic carbons in uniformly labeled peptides and proteins.
  • To adapt solution-state NMR techniques for solid-state applications.

Main Methods:

  • Application of a continuous train of adiabatic inversion pulses in MAS solid-state NMR.

Related Experiment Videos

  • Asynchronous application of adiabatic pulses to facilitate through-bond connectivities, contrasting with rotor-synchronized pulses for dipolar correlations.
  • Utilizing a specific phasing scheme to generate the isotropic mixing Hamiltonian.
  • Employing moderate ¹³C radiofrequency (RF) field strengths.

    • Main Results:

    • Demonstrated efficient scalar coupling-mediated through-bond ¹³C chemical shift correlations for aliphatic carbons.
    • Numerical simulations and experimental measurements confirmed the efficacy of asynchronous adiabatic pulses for mapping through-bond connectivities.
    • The method proved effective for uniformly labeled peptides and proteins.

    Conclusions:

    • The presented MAS solid-state NMR method provides an efficient means to obtain through-bond correlations in peptides and proteins.
    • This technique expands the toolkit for solid-state NMR structural biology, particularly for aliphatic regions.
    • The method's reliance on moderate RF field strengths enhances its practical applicability.