Pressure-stability of phospholipid bicelles: measurement of residual dipolar couplings under extreme conditions.
High-pressure NMR of proteins in solutions currently gains increasing interest. 3D structure determination of proteins under high pressure is, however, so far impossible due to the lack of NOE information. Residual dipolar couplings induced by the addition of magnetically orienting media are known to be capable of replacing NOE information to a very high extent. In the present contribution we study the pressure-stability of dimyristoylphosphatidylcholine (DMPC)/dihexanoylphosphatidylcholine (DHPC) bicelles and demonstrate the feasibility of measuring residual dipolar couplings in proteins under high pressure.
Brunner
E
E
University of Regensburg, Institute of Biophysics and Physical Biochemistry, Germany.
Arnold
M R
MR
Kremer
W
W
Kalbitzer
H R
HR
D007611:Aprotinin / Q000737:chemistry; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D004355:Drug Stability; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010742:Phospholipid Ethers / Q000737:chemistry; D010743:Phospholipids / Q000737:chemistry*; D011312:Pressure; D011506:Proteins / Q000737:chemistry*
C052298:1,2-dihexadecyl-sn-glycero-3-phosphocholine; D008823:Micelles; D010742:Phospholipid Ethers; D010743:Phospholipids; D011506:Proteins; D007611:Aprotinin; D004134:Dimyristoylphosphatidylcholine