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Cited by 275

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles

Open access
Georgieva, Elka R., Ramlall, Trudy F., Borbat, Peter P., Freed, Jack H., Eliezer, David·2008·Journal of the American Chemical Society
DOI 10.1021/ja804517m
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Abstract

We apply pulsed dipolar ESR spectroscopy (Ku-band DEER) to elucidate the global conformation of the Parkinson's disease-associated protein, alpha-synuclein (alphaS) bound to small unilamellar phospholipid vesicles, rodlike SDS micelles, or lipid bicelles. By measuring distances as long as approximately 7 nm between introduced pairs of nitroxide spin labels, we show that distances are close to the expectations for a single continuous helix in all cases studied. In particular, we find distances of 7.5 nm between sites 24 and 72; 5.5 nm between sites 24 and 61; and 2 nm between sites 35 and 50. We conclude that alphaS does not retain a "hairpin" structure with two antiparallel helices, as is known to occur with spheroidal micelles, in agreement with our earlier finding that the protein's geometry is determined by the surface topology rather than being constrained by the interhelix linker. While the possibility of local helix discontinuities in the structure of membrane-bound alphaS remains, our data are more consistent with one intact helix. Importantly, we demonstrate that bicelles produce very similar results to liposomes, while offering a major improvement in experimentally accessible distance range and resolution, and thus are an excellent lipid membrane mimetic for the purpose of pulse dipolar ESR spectroscopy.

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Metadata

Authors
Georgieva, E. R., Ramlall, T. F., Borbat, P. P., Freed, J. H., & Eliezer, D.
Venue
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Published
2008-09-06
Volume
130
Issue
39
Pages
12856-12857
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
DOI
10.1021/ja804517m
OpenAlex
W2026665110
Cited by
275
References
23
FWCI
12.46
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles. https://app.cochat.ai/papers/10.1021/ja804517m
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Georgieva, E. R., Ramlall, T. F., Borbat, P. P., Freed, J. H., & Eliezer, D. (2008). Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles. Journal of the American Chemical Society. https://doi.org/10.1021/ja804517m

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.