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Translational diffusion measurements by microcoil NMR in aqueous solutions of the Fos-10 detergent-solubilized membrane protein OmpX

Academic Article
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Overview

authors

  • Horst, R.
  • Stanczak, P.
  • Serrano-Navarro, Pedro
  • Wuthrich, Kurt

publication date

  • June 2012

journal

  • Journal of Physical Chemistry B  Journal

abstract

  • Aqueous solutions of the detergent Fos-10 (n-decylphosphocholine) without and with addition of the integral membrane protein (IMP) OmpX (outer membrane protein X) have been characterized using pulsed field gradient-stimulated echo (PFG-STE) NMR experiments for measurements of translational diffusion coefficients. Effective diffusion coefficients for Fos-10 micelles in the absence of OmpX were obtained by observation of NMR signals from 10-bromodecan-1-ol that had been inserted into the micelles, and in the presence of OmpX by NMR observation of the protein. It is thus shown that solutions of Fos-10-reconstituted OmpX can be quantitatively described as a mixture of Fos-10 monomers, uniform Fos-10 micelles, and uniform OmpX-containing Fos-10 micelles, with Fos-10 monomers in fast exchange between the pools of these three species. This result establishes an avenue for efficient determination of the effective translational diffusion coefficients of IMP-containing detergent micelles based on observation of the intense detergent NMR signals, which is also applicable with unlabeled IMPs. This monitoring of the species present in a given IMP solution contributes to improved guidelines for rational selection of detergent and buffer conditions in structural studies of integral membrane proteins.

subject areas

  • Bacterial Outer Membrane Proteins
  • Detergents
  • Diffusion
  • Escherichia coli Proteins
  • Hydrolases
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Phosphorylcholine
  • Solubility
  • Solutions
  • Water
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Identity

PubMed Central ID

  • PMC3376199

International Standard Serial Number (ISSN)

  • 1520-6106

Digital Object Identifier (DOI)

  • 10.1021/jp212401w

PubMed ID

  • 22335573
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Additional Document Info

start page

  • 6775

end page

  • 6780

volume

  • 116

issue

  • 23

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