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

在真核生物中，几种膜重塑过程涉及ESCRT-III蛋白，其在细菌中也是保守的。细菌ESCRT-III超家族成员IM 30的单体组装形成大的同源寡聚桶结构，其中单体约80%是α-螺旋。在膜结合时，这些桶分解，并且单体IM 30的C-末端部分展开。在溶液中，低聚受损的IM 30通过相分离过程形成液体冷凝物。我们将使用分子动力学模拟，生物化学和生物物理分析相结合的方法，研究IM 30在溶液中以及膜表面上的α螺旋到无序结构转变。

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.