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α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation

Bernstein, Summer L. and Liu, Dengfeng and Wyttenbach, Thomas and Bowers, Michael T. and Lee, Jennifer C. and Gray, Harry B. and Winkler, Jay R. (2004) α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation. Journal of the American Society for Mass Spectrometry, 15 (10). pp. 1435-1443. ISSN 1044-0305. doi:10.1016/j.jasms.2004.08.003.

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The protein α-synuclein, implicated in Parkinson’s disease, was studied by combining nano-electrospray ionization (N-ESI) mass spectrometry and ion mobility. It was found that both the charge-state distribution in the mass spectra and the average protein shape deduced from ion mobility data, depend on the pH of the spray solution. Negative-ion N-ESI of pH 7 solutions yielded a broad charge-state distribution from −6 to −16, centered at −11, and ion mobility data consistent with extended protein structures. Data obtained for pH 2.5 solutions, on the other hand, showed a narrow charge-state distribution from −6 to −11, centered at −8, and ion mobilities in agreement with compact α-synuclein structures. The data indicated that there are two distinct families of structures: one consisting of relatively compact proteins with eight or less negative charges and one consisting of relatively extended structures with nine or more charges. The average cross section of a-synuclein at pH 2.5 is 33% smaller than for the extended protein sprayed from pH 7 solution. Significant dimer formation was observed when sprayed from pH 7 solution but no dimers were observed from the low pH solution. A plausible mechanism for aggregate formation in solution is proposed.

Item Type:Article
Related URLs:
URLURL TypeDescription ReadCube access
Gray, Harry B.0000-0002-7937-7876
Winkler, Jay R.0000-0002-4453-9716
Additional Information:© 2004 American Society for Mass Spectrometry. Received: 14 April 2004; Revised: 05 August 2004; Accepted: 09 August 2004; First Online: 01 October 2004. This research was supported by a grant from the National Science Foundation, CHE-0140215 (MTB), Beckman Macular Research Center (HBG), Parkinson’s Disease Foundation and National Parkinson Foundation (JRW), and the Beckman Foundation for a Beckman Senior Research Fellowship (JCL).
Funding AgencyGrant Number
Beckman Macular Research CenterUNSPECIFIED
Parkinson’s Disease FoundationUNSPECIFIED
National Parkinson FoundationUNSPECIFIED
Arnold and Mabel Beckman FoundationUNSPECIFIED
Issue or Number:10
Record Number:CaltechAUTHORS:20170530-153130423
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Official Citation:Bernstein, S.L., Liu, D., Wyttenbach, T. et al. J Am Soc Mass Spectrom (2004) 15: 1435. doi:10.1016/j.jasms.2004.08.003
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:77837
Deposited By: Tony Diaz
Deposited On:30 May 2017 22:49
Last Modified:15 Nov 2021 17:34

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