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13C spin dilution for simplified and complete solid-state NMR resonance assignment of insoluble biological assemblies.

A strategy for simplified and complete resonance assignment of insoluble and noncrystalline proteins by solid-state NMR (ssNMR) spectroscopy is presented. Proteins produced with [1-(13)C]- or [2-(13)C]glucose are very sparsely labeled, and the resulting 2D ssNMR spectra exhibit smaller line widths (... Full description

Journal Title: Journal of the American Chemical Society April 6, 2011, Vol.133(13), pp.4722-4725
Main Author: Loquet, Antoine
Other Authors: Lv, Guohua , Giller, Karin , Becker, Stefan , Lange, Adam
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/ja200066s
Link: http://search.proquest.com/docview/859745266/?pq-origsite=primo
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title: 13C spin dilution for simplified and complete solid-state NMR resonance assignment of insoluble biological assemblies.
format: Article
creator:
  • Loquet, Antoine
  • Lv, Guohua
  • Giller, Karin
  • Becker, Stefan
  • Lange, Adam
subjects:
  • Bacterial Proteins–Chemistry
  • Carbon Isotopes–Standards
  • Magnetic Resonance Spectroscopy–Chemistry
  • Nanostructures–Chemistry
  • Particle Size–Chemistry
  • Reference Standards–Chemistry
  • Salmonella Typhimurium–Chemistry
  • Solubility–Chemistry
  • Bacterial Proteins
  • Carbon Isotopes
ispartof: Journal of the American Chemical Society, April 6, 2011, Vol.133(13), pp.4722-4725
description: A strategy for simplified and complete resonance assignment of insoluble and noncrystalline proteins by solid-state NMR (ssNMR) spectroscopy is presented. Proteins produced with [1-(13)C]- or [2-(13)C]glucose are very sparsely labeled, and the resulting 2D ssNMR spectra exhibit smaller line widths (by a factor of ∼2 relative to uniformly labeled proteins) and contain a reduced number of cross-peaks. This allows for an accelerated and straightforward resonance assignment without the necessity of time-consuming 3D spectroscopy or sophisticated pulse sequences. The strategy aims at complete backbone and side-chain resonance assignments based on bidirectional sequential walks. The approach was successfully demonstrated with the de novo assignment of the Type Three Secretion System PrgI needle protein. Using a limited set of simple 2D experiments, we report a 97% complete resonance assignment of the backbone and side-chain (13)C atoms.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/ja200066s
fulltext: no_fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


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title13C spin dilution for simplified and complete solid-state NMR resonance assignment of insoluble biological assemblies.
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subjectBacterial Proteins–Chemistry ; Carbon Isotopes–Standards ; Magnetic Resonance Spectroscopy–Chemistry ; Nanostructures–Chemistry ; Particle Size–Chemistry ; Reference Standards–Chemistry ; Salmonella Typhimurium–Chemistry ; Solubility–Chemistry ; Bacterial Proteins ; Carbon Isotopes
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descriptionA strategy for simplified and complete resonance assignment of insoluble and noncrystalline proteins by solid-state NMR (ssNMR) spectroscopy is presented. Proteins produced with [1-(13)C]- or [2-(13)C]glucose are very sparsely labeled, and the resulting 2D ssNMR spectra exhibit smaller line widths (by a factor of ∼2 relative to uniformly labeled proteins) and contain a reduced number of cross-peaks. This allows for an accelerated and straightforward resonance assignment without the necessity of time-consuming 3D spectroscopy or sophisticated pulse sequences. The strategy aims at complete backbone and side-chain resonance assignments based on bidirectional sequential walks. The approach was successfully demonstrated with the de novo assignment of the Type Three Secretion System PrgI needle protein. Using a limited set of simple 2D experiments, we report a 97% complete resonance assignment of the backbone and side-chain (13)C atoms.
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