血清淀粉样蛋白A天然构象与纤维状构象之间的相互转换。
Interconversion between Serum Amyloid A Native and Fibril Conformations.
作者信息
Yasar Fatih, Sheridan Miranda S, Hansmann Ulrich H E
机构信息
Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
出版信息
ACS Omega. 2022 Mar 30;7(14):12186-12192. doi: 10.1021/acsomega.2c00566. eCollection 2022 Apr 12.
Overexpression of serum amyloid A (SAA) can lead to a form of amyloidosis where the fibrils are made of SAA fragments, most often SAA. Using Replica Exchange with Tunneling, we study the conversion of a SAA chain between the folded conformation and a fibril conformation. We find that the basins in the free energy landscape corresponding to the two motifs are separated by barriers of only about 2-3 . Crucial for the assembly into the fibril structure is the salt bridge 26E-34K that provides a scaffold for forming the fibril conformation.
血清淀粉样蛋白A（SAA）的过表达可导致一种淀粉样变性，其纤维由SAA片段组成，最常见的是SAA。使用隧穿复制交换方法，我们研究了SAA链在折叠构象和纤维构象之间的转变。我们发现，自由能景观中对应于这两种基序的盆地仅由约2-3千卡/摩尔的势垒分隔。对于组装成纤维结构至关重要的是盐桥26E-34K，它为形成纤维构象提供了一个支架。
Zotero 插件