Uversky V N, Li J, Fink A L
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
FEBS Lett. 2001 Nov 30;509(1):31-5. doi: 10.1016/s0014-5793(01)03121-0.
The effect of the natural osmolyte trimethylamine-N-oxide (TMAO) on the structural properties and fibril formation of the natively unfolded protein human alpha-synuclein was studied using several physico-chemical methods. TMAO induced folding of alpha-synuclein: at moderate concentrations, a partially folded intermediate with enhanced propensity for fibrillation accumulated; at higher concentrations, alpha-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.
使用多种物理化学方法研究了天然渗透溶质三甲胺 - N - 氧化物（TMAO）对天然未折叠蛋白人α - 突触核蛋白的结构特性和纤维形成的影响。TMAO诱导α - 突触核蛋白折叠：在中等浓度下，积累了具有增强纤维化倾向的部分折叠中间体；在较高浓度下，α - 突触核蛋白紧密折叠并发生自缔合形成寡聚体。后一种构象具有明显的螺旋结构，可能代表该蛋白的生理折叠形式。
