Moshe Asher, Landau Meytal, Eisenberg David
Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Department of Biological Chemistry, Howard Hughes Medical Institute (HHMI), University of California Los Angeles (UCLA), 611 Charles Young Dr. East, Los Angeles, CA, 90095-1569, USA.
Methods Mol Biol. 2016;1345:201-10. doi: 10.1007/978-1-4939-2978-8_13.
The molecular structures of amyloid fibers and oligomers are required in order to understand and control their formation. Yet, their partially disordered and polymorphic nature hinders structural analyses. Fortunately, short segments from amyloid proteins, which exhibit similar biophysical properties to the full-length proteins, also form fibrils and oligomers and their atomic structures can be determined. Here we describe experimental procedures used to assess fiber-forming capabilities of amyloid peptide segments and their crystallization.
为了理解和控制淀粉样纤维和寡聚体的形成,需要了解它们的分子结构。然而,它们部分无序和多态的性质阻碍了结构分析。幸运的是,淀粉样蛋白的短片段与全长蛋白具有相似的生物物理特性,也能形成纤维和寡聚体,并且可以确定它们的原子结构。在这里,我们描述了用于评估淀粉样肽段形成纤维的能力及其结晶的实验程序。