Abstract
Dipolar waves are distinct hallmarks of both the secondary and tertiary structures of α-helical proteins that are immobilized in membrane bilayers or embedded in anisotropic media. We present a simple, semi-empirical approach that exploits the modulation of the amplitude and average of dipolar waves to determine the topology of α-helical proteins. Moreover, we describe the application of this method for the structural determination of a detergent solubilized membrane protein, phospholamban (PLB) that is involved in calcium regulation of cardiac muscle. When combined with high-resolution solid-state NMR data, this method can serve as a fast route for determining the topology of helical membrane proteins solubilized in detergent micelles.
Original language | English (US) |
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Pages (from-to) | 133-144 |
Number of pages | 12 |
Journal | Chemistry and Physics of Lipids |
Volume | 132 |
Issue number | 1 |
DOIs | |
State | Published - Oct 2004 |
Bibliographical note
Funding Information:This work was supported in part by grants to G.V. (NIH GM64742; AHA 0160465Z). The authors would like to thank Dr. S.J. Opella, Francesca Marassi, Michael Mesleh for many helpful discussions, Roberto Di Fonzo for encouragement and support, David Live and Beverly Ostrowski for help with NMR experiments. We also benefited from the facilities at the Minnesota High-Field NMR Center in the Department of Biochemistry, Molecular Biology, and Biophysics; University of Minnesota. NMR instrumentation was provided with funds from the NSF (BIR-961477) and the University of Minnesota Medical School.
Keywords
- Ca-ATPase
- DPC micelles
- Dipolar waves
- Exhaustive search
- Helical wheels
- Membrane proteins
- NMR
- Phospholamban
- Polyacrylamide gel
- Residual dipolar couplings
- SERCA
- α-Helix