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Related Experiment Video

Updated: Jun 2, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Membrane protein structure determination using paramagnetic tags.

Soumya Ganguly¹, Brian E Weiner, Jens Meiler

¹Departments of Chemistry, Pharmacology, and Biomedical Informatics, Center for Structural Biology, Institute for Chemical Biology, Vanderbilt University, 7330 Stevenson Center, Station B 351822, Nashville, TN 37235, USA.

Structure (London, England : 1993)

|April 13, 2011

Summary

This summary is machine-generated.

Paramagnetic tagging combined with NMR or EPR spectroscopy can revolutionize helical membrane protein structure determination. Optimal labeling and topology prediction are key to unlocking this technique's full potential for structural biology.

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Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

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Last Updated: Jun 2, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

Area of Science:

Biophysics
Structural Biology
Biochemistry

Background:

Helical membrane proteins are crucial in biological processes but challenging to study structurally.
Paramagnetic tagging combined with Nuclear Magnetic Resonance (NMR) or Electron Paramagnetic Resonance (EPR) spectroscopy offers a powerful approach for de novo structure determination.

Discussion:

This work addresses the need for optimal labeling strategies in paramagnetic tagging.
It highlights the importance of predicting membrane protein topology from sparse, low-resolution distance restraints.

Key Insights:

The integration of paramagnetic tagging with NMR/EPR spectroscopy can significantly advance the de novo structure determination of helical membrane proteins.
Effective structure elucidation relies on sophisticated labeling techniques and accurate topological predictions.

Outlook:

Further development in labeling strategies and computational methods will enhance the application of these spectroscopic techniques.
This approach holds promise for detailed structural insights into membrane protein function and drug discovery.