Exploration of the Biomaterial Properties and Applications of Ure2 Amyloid Fibrils

来源 :第四届全国冷冻电子显微学与结构生物学专题研讨会 | 被引量 : 0次 | 上传用户：zhouyonge

【摘要】

：

Amyloid fibrils are highly ordered protein aggregates formed by self-assembly of proteins.Amyloids exist broadly in nature from prokaryotic organisms to mammals

【作者】

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Xiao-ming Zhou Elizabeth Sawyer Ulyana Shimanovich Tuomas Knowles Sarah Perrett

【机构】

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InstituteofBiophysics,ChineseAcademyofSciences,Beijing,ChinaDepartmentofChemistry,UniversityofCambri

【出处】

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第四届全国冷冻电子显微学与结构生物学专题研讨会

【发表日期】

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2015年6期

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Amyloid fibrils are highly ordered protein aggregates formed by self-assembly of proteins.Amyloids exist broadly in nature from prokaryotic organisms to mammals and are associated not only with neurodegenerative disorders of mammals but also with function roles in bacteria and other organisms.In addition to their nano-scale size,the extraordinary stability and tunable assembly of amyloid fibrils make them attractive targets as nanomaterials.

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Exploration of the Biomaterial Properties and Applications of Ure2 Amyloid Fibrils

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