Intrinstically Disordered Protein, Folding, Aggregation and Intermolecular Interactions
|摘要:||無穩定構型蛋白質(Intrinsically disordered protein)為蛋白質交互作用網絡之核心。然
而其穩定予否則端賴其是否摺疊正確。蛋白質摺疊似一階態轉變(first order-like state
點。此外透過量測intrinsically disordered protein 之Raman 與螢光光譜於摺疊中間體之
蛋白質之聚集沉澱符合摺疊與擴散速率限制聚集(diffusion limited aggregation)相拮抗
Intrinsically disordered protein plays a vital role in the networks of protein-protein interactions. However, their stabilities rely on the process of folding. The first order-like state transition model is the proper model to describe the global reaction of protein folding. However, the folding reaction of intrinsically disordered protein remains unknown. Therefore, one of the aims of this project is focusing on the mechanisms study of intrinsically disordered proteins folding and their interactions. Meanwhile, the “first order-like state transition model” will be examined in this project. By using Raman and fluorescence spectroscopy analysis of their folding intermediates, the folding cores of intrinsically disordered protein can be revealed. Meanwhile, the major affecting factors of folding transition region/boundary can be determined by systematically folding studies. These affecting factors may help us to reveal the protein aggregation mechanism. Meanwhile, we will test the competitive model of protein folding and diffusion limited aggregation in this project. In order to reveal the self-assembly mechanism of intrinsically disordered protein, in this project, we will use the molecular dielectrophoresis driven self-assembly method, which developed my laboratory, and make the protein aggregated in the nano-pattern of silicon substrates. Furthermore, the conformation of aggregated protein will be revealed by atomic force microsopy and cryo-transmitted electron microscopy. Meanwhile, the dynamics of this protein aggregation and conformation transition of the loop region during protein-protein interactions can be revealed by optical combining single molecular manipulation methods which development by my laboratory.
|Appears in Collections:||Research Plans|