Trimethylamine-n-oxide-induced Folding of α-synuclein
Document Type
Article
Publication Date
2001
Digital Object Identifier (DOI)
https://doi.org/10.1016/S0014-5793(01)03121-0
Abstract
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.
Citation / Publisher Attribution
FEBS Letters, v. 509, issue 1, p. 31-35
Scholar Commons Citation
Uversky, Vladimir N.; Li, Jie; and Fink, Anthony L., "Trimethylamine-n-oxide-induced Folding of α-synuclein" (2001). Molecular Medicine Faculty Publications. 678.
https://digitalcommons.usf.edu/mme_facpub/678
