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

在真核生物中，一些膜重塑过程涉及ESCRT-III蛋白，该蛋白在细菌中也保守。细菌ESCRT-III超家族成员IM30的单体组装形成大的同质寡聚桶状结构，其中单体为~80%的α -螺旋结构。膜结合后，这些桶拆卸，单体IM30的c端部分展开。在溶液中，寡聚受损的IM30通过相分离过程形成液态凝聚物。我们将利用分子动力学模拟、生化和生物物理分析相结合的方法，研究IM30在溶液和膜表面上从α -螺旋到无序结构的转变。

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.