Nanopore analysis of protein structure and folding

在健康的细胞中，大多数蛋白质在合成后不久就会折叠成特定的结构或构象。当不再需要时，蛋白质分解，氨基酸构建块被重新使用以制造新的蛋白质。在某些病理条件下，正常的合成和更新过程发生故障，错误折叠的蛋白质可以开始积累。错误折叠的蛋白质是不寻常的，因为它们很难降解，它们的存在最终会干扰关键的细胞功能，导致细胞死亡。错误折叠的蛋白质通常聚集成“淀粉样斑块”，这可以在显微镜下识别。大脑中淀粉样蛋白斑块的存在是许多神经退行性疾病的标志，如阿尔茨海默氏症和帕金森氏症。虽然引起这些疾病的蛋白质是已知的，但它们错误折叠的原因还不清楚。

In a healthy cell, most proteins fold into a specific structure or conformation soon after they are synthesized. When no longer needed, the proteins break down and the amino acid building blocks are reused to make new proteins. Under certain pathological conditions, the normal process of synthesis and renewal malfunctions and misfolded proteins can begin to accumulate. Misfolded proteins are unusual because they are difficult to degrade and their presence eventually interferes with critical cell functions and the cell dies. The misfolded proteins often aggregate into "amyloid plaques", which can be identified under a microscope. The presence of amyloid plaques in the brain is the hallmark of many neurodegenerative diseases, such as Alzheimer's and Parkinson's. Although the proteins that cause these diseases are known, the reasons why they misfold are not well understood.