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Lipid-protein interactions in dhpc micelles containing the integral membrane protein ompx investigated by NMR spectroscopy

Academic Article
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Overview

authors

  • Fernandez, C.
  • Hilty, C.
  • Wider, G.
  • Wuthrich, Kurt

publication date

  • October 2002

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Intermolecular nuclear Overhauser effects (NOEs) between the integral outer membrane protein OmpX from Escherichia coli and dihexanoylphosphatidylcholine (DHPC) provided a detailed description of protein-detergent interactions. The NOEs were measured in 3D (15)N- and (13)C-resolved [(1)H,(1)H]-NOESY spectra recorded with selectively methyl-protonated and otherwise uniformly (2)H,(13)C,(15)N-labeled OmpX in micelles of DHPC at natural isotope abundance. In these mixed micelles the NMR structure of OmpX consists of an eight-stranded antiparallel beta-barrel. The OmpX surface area covered with intermolecular NOEs to the DHPC hydrophobic tails forms a continuous cylinder jacket of approximately 28 A in height, which is centered about the middle of the long axis through the beta-barrel. In addition, some intermolecular NOEs with methyl groups of the DHPC polar head were identified along both boundaries of this cylinder jacket. The experimental data suggest that the hydrophobic surface areas of OmpX are covered with a monolayer of DHPC molecules, which appears to mimic quite faithfully the embedding of the beta-barrel in a double-layer lipid membrane.

subject areas

  • Bacterial Outer Membrane Proteins
  • Crystallography, X-Ray
  • Detergents
  • Escherichia coli Proteins
  • Hydrolases
  • Hydrophobic and Hydrophilic Interactions
  • Membrane Lipids
  • Micelles
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Phosphatidylcholines
  • Protein Conformation
  • Protein Structure, Secondary
  • Protons
  • Recombinant Proteins
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Research

keywords

  • NOE
  • detergents
  • intermolecular NOEs
  • solvation of membrane proteins
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Identity

PubMed Central ID

  • PMC129708

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.212515099

PubMed ID

  • 12370417
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Additional Document Info

start page

  • 13533

end page

  • 13537

volume

  • 99

issue

  • 21

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