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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Bicelle samples for solid-state NMR of membrane proteins
Anna A De Angelis1, Stanley J Opella
1Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, California 92037, USA.
Nature Protocols
|October 20, 2007
Summary
Magnetically aligned bicelles enable high-resolution solid-state NMR for membrane protein structure determination. This method ensures proteins remain functional in hydrated bilayers, facilitating detailed structural analysis.
Area of Science:
- Biophysics
- Structural Biology
- Biochemistry
Background:
- Bicelles, mixtures of long- and short-chain phospholipids, form hydrated bilayers in aqueous solutions.
- These bicelles align spontaneously in high magnetic fields (400-900 MHz NMR), creating an ideal environment for solid-state NMR spectroscopy.
- Membrane proteins retain full functionality under physiological conditions within these bicelle environments.
Purpose of the Study:
- To describe a protocol for preparing stable, protein-containing bicelle samples.
- To demonstrate the utility of magnetically aligned bicelles for structure determination of membrane proteins using solid-state NMR.
- To highlight the high-resolution spectral data achievable with this method.
Main Methods:
- Preparation of magnetically aligned bicelle samples containing isotopically labeled membrane proteins.
- Utilizing solid-state NMR spectroscopy for structural analysis.
- Maintaining physiological conditions (pH, temperature) for protein functionality.
Main Results:
- Achieved high-resolution solid-state NMR spectra from membrane proteins within bicelles.
- Demonstrated the stability of protein-containing bicelle samples.
- Confirmed the functionality of membrane proteins in the bicelle environment.
Conclusions:
- Magnetically aligned bicelles are a robust and effective medium for membrane protein structure determination via solid-state NMR.
- The protocol allows for the preparation of samples yielding high-quality NMR spectra.
- Sample preparation time varies based on protein characteristics, ranging from hours to days.
