In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells

α-Synuclein is a small protein strongly implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders. We report here the use of in-cell NMR spectroscopy to observe directly the structure and dynamics of this protein within E. coli cells. To improve the accuracy...

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Published in:PloS one 2013-08, Vol.8 (8), p.e72286-e72286
Main Authors: Waudby, Christopher A, Camilloni, Carlo, Fitzpatrick, Anthony W P, Cabrita, Lisa D, Dobson, Christopher M, Vendruscolo, Michele, Christodoulou, John
Format: Article
Language:English
Subjects:
alpha-Synuclein - chemistry
Bacteria
Chemistry
Cytosol
E coli
Escherichia coli - chemistry
Experiments
Line broadening
Magnetic resonance spectroscopy
Molecular biology
Neurodegenerative diseases
NMR
NMR spectroscopy
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular - methods
Pathogenesis
Populations
Protein structure
Protein Structure, Secondary
Proteins
Secondary structure
Spectroscopy
Structural analysis
Synuclein
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description α-Synuclein is a small protein strongly implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders. We report here the use of in-cell NMR spectroscopy to observe directly the structure and dynamics of this protein within E. coli cells. To improve the accuracy in the measurement of backbone chemical shifts within crowded in-cell NMR spectra, we have developed a deconvolution method to reduce inhomogeneous line broadening within cellular samples. The resulting chemical shift values were then used to evaluate the distribution of secondary structure populations which, in the absence of stable tertiary contacts, are a most effective way to describe the conformational fluctuations of disordered proteins. The results indicate that, at least within the bacterial cytosol, α-synuclein populates a highly dynamic state that, despite the highly crowded environment, has the same characteristics as the disordered monomeric form observed in aqueous solution.
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subjects alpha-Synuclein - chemistry
Bacteria
Chemistry
Cytosol
E coli
Escherichia coli - chemistry
Experiments
Line broadening
Magnetic resonance spectroscopy
Molecular biology
Neurodegenerative diseases
NMR
NMR spectroscopy
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular - methods
Pathogenesis
Populations
Protein structure
Protein Structure, Secondary
Proteins
Secondary structure
Spectroscopy
Structural analysis
Synuclein
title In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells
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