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Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles

Academic Article
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Overview

authors

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

publication date

  • 2012

journal

  • Journal of Biomolecular NMR  Journal

abstract

  • Optimization of aqueous solutions of the integral membrane protein (IMP) OmpW for NMR structure determination has been monitored with micro-coil NMR, which enables the acquisition of NMR spectra using only micrograms of protein and detergent. The detergent 30-Fos (2-undecylphosphocholine) was found to yield the best 2D [(15)N, (1)H]-TROSY correlation NMR spectra of [(2)H, (15)N]-labeled OmpW. For the OmpW structure determination we then optimized the 30-Fos concentration, the sample temperature and long-time stability, and the deuteration level of the protein. Some emerging guidelines for reconstitution of β-barrel integral membrane proteins in structural biology are discussed.

subject areas

  • Bacterial Outer Membrane Proteins
  • Detergents
  • Deuterium
  • Escherichia coli Proteins
  • Micelles
  • Phosphorylcholine
  • Protein Conformation
  • Protein Stability
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Research

keywords

  • E. coli outer membrane protein W
  • Integral membrane proteins
  • Solubilization in detergent micelles
  • Structural biology
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Identity

PubMed Central ID

  • PMC3715323

International Standard Serial Number (ISSN)

  • 0925-2738

Digital Object Identifier (DOI)

  • 10.1007/s10858-012-9658-x

PubMed ID

  • 22890565
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Additional Document Info

start page

  • 129

end page

  • 133

volume

  • 54

issue

  • 2

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