Pan Yangang, Wang Bin, Zhang Tong, Zhang Yanan, Wang Hongda, Xu Bingqian
Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA.
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, P. R. China.
Chem Commun (Camb). 2016 Jun 30;52(55):8533-6. doi: 10.1039/c6cc03029g.
The aggregates of the full-length human recombinant prion protein (PrP) (23-231) on model membranes were investigated by combining the atomic force microscopy (AFM) measurements and theoretical calculations at pH 5.0, showing the great effect of PrP concentration on its supramolecular assemblies on the lipid bilayer.
通过结合原子力显微镜（AFM）测量和理论计算，研究了全长人重组朊病毒蛋白（PrP）（23 - 231）在pH 5.0的模型膜上的聚集体，结果表明PrP浓度对其在脂质双层上的超分子组装有很大影响。
