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Related Experiment Video

Updated: Jun 28, 2026

Experimental Methods for Spin- and Angle-Resolved Photoemission Spectroscopy Combined with Polarization-Variable Laser
09:00

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14N Polarization Inversion Spin Exchange at Magic Angle (PISEMA).

Chunqi Qian1, Riqiang Fu, Peter Gor'kov

  • 1Center for Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, Tallahassee, FL 32310, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|November 7, 2008
PubMed
Summary

We introduce a new (14)N-PISEMA experiment for peptide orientation analysis in aligned samples. This method uses natural abundant nitrogen and (14)N quadrupolar coupling for sensitive orientation determination.

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Structural biology and biophysics.

Background:

  • Determining peptide orientation in aligned samples, like membranes, is crucial for understanding their function.
  • Existing methods may require isotope enrichment, increasing costs and complexity.

Purpose of the Study:

  • To present a novel (14)N-PISEMA experiment for sensitive peptide orientation determination.
  • To enable orientation analysis without isotopic enrichment of nitrogen.

Main Methods:

  • Development and application of the (14)N-PISEMA experiment.
  • Correlation of (14)N quadrupolar coupling and (14)N-(1)H dipolar coupling.
  • Selective spin-exchange between protons and (14)N single-quantum transitions.

Main Results:

  • Demonstration of the (14)N-PISEMA experiment on a natural abundant N-acetyl valine crystal.
  • Validation of (14)N quadrupolar coupling tensor as a sensitive probe for peptide orientation.
  • Successful orientation determination without isotope enrichment.

Conclusions:

  • The (14)N-PISEMA experiment is a powerful, cost-effective tool for peptide orientation studies.
  • This method enhances the utility of solid-state NMR for structural biology.
  • The technique is applicable to uniformly aligned biological samples.