FEBS Letters | |
Trimethylamine‐N‐oxide‐induced folding of α‐synuclein | |
Fink, Anthony L.1  Uversky, Vladimir N.1  Li, Jie1  | |
[1] Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA | |
关键词: α-Synuclein; Fibril; Osmolyte; Natively unfolded; Trimethylamine-N-oxide; Oligomer; | |
DOI : 10.1016/S0014-5793(01)03121-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The effect of the natural osmolyte trimethylamine-N-oxide (TMAO) on the structural properties and fibril formation of the natively unfolded protein human α-synuclein was studied using several physico-chemical methods. TMAO induced folding of α-synuclein: at moderate concentrations, a partially folded intermediate with enhanced propensity for fibrillation accumulated; at higher concentrations, α-synuclein was tightly folded and underwent self-association to form oligomers. The latter conformation was significantly helical and probably represents the physiologically folded form of the protein.
【 授权许可】
Unknown
【 预 览 】
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