Interactions with hydrophobic clusters in the urea-unfolded membrane protein OmpX.
Hiller
Sebastian
S
Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Wider
Gerhard
G
Imbach
Lukas L
LL
Wüthrich
Kurt
K
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D003902:Detergents / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006867:Hydrolases / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D009682:Magnetic Resonance Spectroscopy / Q000379:methods / Q000592:standards; D008823:Micelles; D008958:Models, Molecular; D010742:Phospholipid Ethers / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D012015:Reference Standards; D014508:Urea / Q000737:chemistry*
C052298:1,2-dihexadecyl-sn-glycero-3-phosphocholine; D001425:Bacterial Outer Membrane Proteins; D003902:Detergents; D029968:Escherichia coli Proteins; D008823:Micelles; D010742:Phospholipid Ethers; C482905:OmpX protein, E coli; D014508:Urea; D006867:Hydrolases