Control of Protein Folding and Protein Self Assembling through Fluorine-Specific Interactions (A04)

通过氟特异性相互作用控制蛋白质折叠和蛋白质自组装 (A04)

• 批准号: 414779062
• 金额: --
• 依托单位: Abteilung Organische Chemie
• 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/414779062?language=en
• 关键词: Control; Protein; Folding; Self; Assembling

A4|Koksch deals with the segregation properties of fluorinated groups with respect to protein folding. For this, fluorinated amino acids will be incorporated into beta-sheet domains of proteins. Furthermore, the formation of networks between fluorinated derivatives of the serine-protease-inhibitor BPTI with the proteases β-trypsin and α-chymotrypsin as well as the protein-inhibitor-complex barnase/barstar are investigated. Finally, the abil-ity for self-assembly of novel, highly fluorinated model peptides and their interaction with model membranes (SDS, POPC/POPG) and intact cells is studied.

A4| Koksch研究了氟化基团在蛋白质折叠中的分离特性。为此，氟化氨基酸将被掺入蛋白质的β折叠结构域中。此外，研究了丝氨酸蛋白酶抑制剂BPTI的氟化衍生物与蛋白酶β-胰蛋白酶和α-胰凝乳蛋白酶以及蛋白质抑制剂复合物芽孢杆菌RNA酶/芽孢杆菌RNA酶抑制剂之间的网络形成。最后，研究了新型高氟化模型肽的自组装能力及其与模型膜（SDS，POPC/POPG）和完整细胞的相互作用。