Intrinsically Disordered to α-Helix Transition of the IM30 Protein Structure (R01)

IM30 蛋白质结构 (R01) 本质上无序到 α 螺旋转变

• 批准号: 518273526
• 金额: --
• 依托单位: Max-Planck-Institut für Polymerforschung
• 依托单位国家: 德国
• 项目类别: Collaborative Research Centres
• 资助国家: 德国
• 项目状态: 未结题
• 来源: https://gepris.dfg.de/gepris/projekt/518273526?language=en
• 关键词: Intrinsically; Disordered; Helix; Transition; IM30

In eukaryotes, several membrane remodeling processes involve ESCRT-III proteins, which are also conserved in bacteria. Monomers of the bacterial ESCRT-III superfamily member IM30 assemble to form large homo-oligomeric barrel structures, where the monomers are ~80% α‑helical. Upon membrane binding, these barrels disassemble, and the C-terminal part of monomeric IM30 unfolds. In solution, oligomerization-impaired IM30 forms liquid condensates by a phase separation process. We will study the α‑helix-to-disordered structural transition of IM30 in solution as well as on membranes surfaces, using a combination of molecular dynamics simulations, biochemical and biophysical analyses.

在真核生物中，一些膜重塑过程涉及ESCRT-III蛋白，这些蛋白在细菌中也是保守的。细菌ESCRT-III超家族成员IM30的单体聚集形成大的同源低聚桶状结构，其中单体约80%是α-螺旋的。当膜结合时，这些桶解体，单体IM30的C-末端部分展开。在溶液中，低聚损伤的IM30通过相分离过程形成液体冷凝物。我们将结合分子动力学模拟、生化和生物物理分析，研究IM30在溶液和膜表面的α-螺旋到无序结构的转变。