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Probing Structural Changes in Alpha-Synuclein by Nuclear Magnetic Resonance Spectroscopy

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Alpha-Synuclein

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1948))

Abstract

Alpha-synuclein, the principal protein involved in the pathogenesis of Parkinson’s disease, has been shown to exchange between multiple conformational states, with hitherto unclear physiological role of such conformational changes. Due to its ability to provide rich structural information for proteins in their near-native environment, nuclear magnetic resonance (NMR) spectroscopy has been a valuable tool to study these conformational states. In this review we describe the application of model systems and NMR methods to the study of membrane-bound states of alpha-synuclein. We provide a detailed description, primarily meant for someone new to the field, of how to prepare the necessary samples, perform the basic experiments, and obtain an initial interpretation of the results.

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Authors and Affiliations

  1. Weill Cornell Medicine, New York, NY, USA

    Tapojyoti Das & David Eliezer

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  1. Tapojyoti Das
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  2. David Eliezer
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Correspondence to David Eliezer .

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Editors and Affiliations

  1. Dementia Research Institute, University College London, London, UK

    Tim Bartels

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Das, T., Eliezer, D. (2019). Probing Structural Changes in Alpha-Synuclein by Nuclear Magnetic Resonance Spectroscopy. In: Bartels, T. (eds) Alpha-Synuclein. Methods in Molecular Biology, vol 1948. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9124-2_13

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  • DOI: https://doi.org/10.1007/978-1-4939-9124-2_13

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-9123-5

  • Online ISBN: 978-1-4939-9124-2

  • eBook Packages: Springer Protocols

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