Application of NMR in the Studies of Structure and Interactions of α-Synuclein

doi:10.11938/cjmr20160115

Abstract

Abstract:

α-synuclein (AS) is natively unfolded protein, and has the potential to aggregate and assemble into fibrils. AS fibril is the major component of Lewy bodies (LB), the hallmark of neurodegenerative diseases such as Parkinson's disease (PD). Many previous studies have studied the structure and functions of AS, hoping toshed a light on the pathogenesis of PD. Compared to the other methods, nuclear magnetic resonance (NMR) has many advantages in studying natively unfolded proteins, and can provide atom-level structural and dynamic information of these proteins. This review focuses on the applications of NMR, combined with other techniques, in the studies on the structure, aggregation mechanisms, membrane interactions, metal ion interactions, and protein interactions of AS.

Key words: NMR, α-synuclein, protein structure, protein fibrillation, protein interaction

CLC Number:

O482.53

DAI Chen-ye, ZHANG Ze-ting, LIU Mai-li, LI Cong-gang. Application of NMR in the Studies of Structure and Interactions of α-Synuclein[J]. Chinese Journal of Magnetic Resonance, 2016, 33(1): 153-167.

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