Uncovering amyloid formation mechanism of yeast prion Ure2 by single molecule FRET and kinetic analy

来源 :中国化学会生物物理化学专业委员会第四届全国生物物理化学会议 | 被引量 : 0次 | 上传用户：yuhan78001

【摘要】

：

　　Protein aggregation to form amyloid fibrils is associated with a variety of neurodegenerative diseases,in which oligomeric intermediates formed during the e

【作者】

：

杨洁 DearAlexander KnowlesTuomas P.J. 吴思 PerrettSarah

【机构】

：

NationalLaboratoryofBiomacromolecules,InstituteofBiophysics,ChineseAcademyofSciencesDepartmentofChem

【出处】

：

中国化学会生物物理化学专业委员会第四届全国生物物理化学会议

【发表日期】

：

2016年6期

【关键词】

：

Ure2 amyloid formation oligomeric intermediate single molecule FRET

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　　Protein aggregation to form amyloid fibrils is associated with a variety of neurodegenerative diseases,in which oligomeric intermediates formed during the early stages cause neurotoxicity to cells.Due to the low-populated,metastable and heterogeneous nature of oligomers,it is hard to determine the conformation details and microscopic reactions during oligomeric assembly.

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Uncovering amyloid formation mechanism of yeast prion Ure2 by single molecule FRET and kinetic analy

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