Biochemistry and Structural Biology, Lund University, Lund, Sweden.
Methods Mol Biol. 2020;2141:731-754. doi: 10.1007/978-1-0716-0524-0_38.
High purity and sequence homogeneity of intrinsically disordered proteins are prerequisites for reproducible studies of the kinetics and equilibrium of their self-assembly reactions. Starting from the pure state enables quantitative studies of intrinsic and extrinsic factors in the process to understand its molecular determinants. Here we outline detailed protocols for recombinant expression and purification of ultra-pure amyloid β peptide (Aβ) in sequence homogeneous form, which allows for the setup of reproducible kinetic self-assembly experiments.
高纯度和序列均一性是重现性研究其自组装反应动力学和平衡的先决条件。从纯态开始可以定量研究过程中的内在和外在因素，以了解其分子决定因素。在这里，我们概述了详细的重组表达和超纯淀粉样β肽（Aβ）的纯化方案，该方案可实现可重现的动力学自组装实验。
