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In-Cell NMR Characterization of the Secondary Structure Populations of a Disordered Conformation of α-Synuclein within E. coli Cells.

Waudby, CA; Camilloni, C; Fitzpatrick, AW; Cabrita, LD; Dobson, CM; Vendruscolo, M; Christodoulou, J; (2013) In-Cell NMR Characterization of the Secondary Structure Populations of a Disordered Conformation of α-Synuclein within E. coli Cells. PLoS One , 8 (8) , Article e72286. 10.1371/journal.pone.0072286. Green open access

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Abstract

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.

Type: Article
Title: In-Cell NMR Characterization of the Secondary Structure Populations of a Disordered Conformation of α-Synuclein within E. coli Cells.
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1371/journal.pone.0072286
Publisher version: http://dx.doi.org/10.1371/journal.pone.0072286
Language: English
Additional information: ©� 2013 Waudby et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/1403232
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