Chinese Journal of Magnetic Resonance >
Salt Content-Dependent Conformational Changes of α-Synuclein Studied by 19F NMR
Received date: 2014-05-05
Revised date: 2015-01-11
Online published: 2015-03-05
Supported by
国家自然科学基金资助项目(21173258), 国家重点基础研究发展计划(“973 计划”)资助项目(2013CB910200).
α-synuclein is an intrinsically disordered protein, and is implicated in Parkinson's disease. Previous studies have found that the aggregation rate, fibril structure, propagation and cytotoxicity of α-synuclein change markedly with salt concentration. However, the underlying molecular mechanisms remain poorly understood. In this work, 3-fluorotyrosine (3FY) labeling was introduced into α-synuclein, and the conformational changes of the protein under different salt concentrations were studied by 19F NMR. It was found that the protein was more compact at low salt concentration than at high salt
concentration; and such conformational changes may account for the fibril morphology diversity and physiological effects of the protein at different salt concentrations. It was also concluded that 19F NMR is a sensitive technique to measure conformational change of intrinsically disordered protein.
Key words： liquid-state NMR; 19F NMR; intrinsically disordered proteins; α-synuclein
DAI Chen-ye1 , 2 , LIU Mai-li1 , LI Cong-gang1 . Salt Content-Dependent Conformational Changes of α-Synuclein Studied by 19F NMR[J]. Chinese Journal of Magnetic Resonance, 2015 , 32(1) : 33 -40 . DOI: 10.11938/cjmr20150104
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