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Smaller Nanodiscs are Suitable for Studying Protein Lipid Interactions by Solution NMR
Xiaoming Wang1, Zongjun Mu, Yan Li
1High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Science, Hefei, 230031, Anhui, China.
The Protein Journal
|May 19, 2015
Summary
Researchers developed smaller phospholipid bilayer nanodiscs for studying membrane proteins. These nanodiscs, using a modified scaffold protein, maintain a native-like environment suitable for solution NMR studies of proteins like STIM1-TM.
Area of Science:
- Biochemistry
- Structural Biology
- Membrane Biophysics
Background:
- Phospholipid bilayer nanodiscs offer a native-like environment for studying membrane proteins.
- Nanodisc size is tunable by modifying the membrane scaffold protein (MSP).
Purpose of the Study:
- To express and purify a deletion mutant of MSP (ΔMSP).
- To characterize smaller nanodiscs assembled with ΔMSP and mixed lipids.
- To assess the utility of these smaller nanodiscs for membrane protein studies using solution NMR.
Main Methods:
- Expression and purification of the ΔMSP mutant.
- Assembly of nanodiscs using ΔMSP and mixed lipids.
- Analysis of nanodisc structure and lipid environment using (31)P NMR.
- Incorporation and study of STIM1-Transmembrane (STIM1-TM) domain.
Main Results:
- Successfully expressed and purified ΔMSP.
- Assembled smaller nanodiscs with mixed lipids.
- NMR data indicated similar chemical environments to larger nanodiscs.
- Demonstrated successful incorporation of STIM1-TM into the smaller nanodiscs.
Conclusions:
- The ΔMSP mutant enables the creation of smaller nanodiscs.
- These smaller nanodiscs maintain a native-like lipid environment.
- The system is suitable for membrane protein studies, including STIM1-TM, via solution NMR.
