Interactions with hydrophobic clusters in the urea-unfolded membrane protein OmpX

Angew Chem Int Ed Engl. 2008;47(5):977-81. doi: 10.1002/anie.200703367.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Detergents / chemistry
  • Escherichia coli Proteins / chemistry*
  • Hydrolases / chemistry*
  • Hydrophobic and Hydrophilic Interactions
  • Magnetic Resonance Spectroscopy / methods
  • Magnetic Resonance Spectroscopy / standards
  • Micelles
  • Models, Molecular
  • Phospholipid Ethers / chemistry
  • Protein Denaturation
  • Protein Folding
  • Reference Standards
  • Urea / chemistry*

Substances

  • 1,2-dihexadecyl-sn-glycero-3-phosphocholine
  • Bacterial Outer Membrane Proteins
  • Detergents
  • Escherichia coli Proteins
  • Micelles
  • Phospholipid Ethers
  • OmpX protein, E coli
  • Urea
  • Hydrolases