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

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
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金额:
$0.0万
依托单位国家:
德国
项目类别:
Collaborative Research Centres
财政年份:
--
资助国家:
德国
项目状态:
未结题
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英文摘要
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.
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