小窩蛋白-1在不對(duì)稱雙層膜模型中的動(dòng)力學(xué)行為研究
[Abstract]:Vesicles are asymmetric bilayer membrane structures rich in sphingolipids and cholesterol on the cell membrane. They are involved in many biological processes such as signal transduction endocytosis lipid transport and so on. Fossa protein is the basic protein of small nest. The dysfunction and misregulation of nest protein are related to the occurrence of many major diseases, so the study of nest protein is of great significance. However, the structure of fossa protein has not been elucidated and its conformation in the fossa is unclear. Fossa protein-1 is the earliest found and most widely distributed fossa protein subtype, and is also a cholesterol binding protein. In this paper, the kinetic behavior of fosin-1 in asymmetric phospholipid bilayer membrane was studied. In the second chapter, a bilayer membrane model with different phospholipid composition in the inner and outer membrane was built, and the stability of the model was verified by molecular dynamics simulation. In the third chapter, based on the second chapter, the complex system of small nest protein-1 (residue 82-136) and asymmetric bilayer membrane model is built, and the molecular dynamics simulation is carried out by two one-microsecond molecular models. We found that the scaffold region of fossa protein-1 (residue 82-101) can form a complete a-helix structure with a part of the transmembrane region (residue 102-107). Fossa protein-1 (residue 82-136) can exist stably in the membrane with "U" conformation. In the simulation, fosin-1 (residue 82-136) was inserted only into the inner membrane of the asymmetric bilayer membrane, which could increase the order of the membrane phospholipid molecule and decrease the order of the outer membrane phospholipid molecule. In addition, no cholesterol tendentiousness binding site was found in the scaffold area of fossa-1.
【學(xué)位授予單位】:華東理工大學(xué)
【學(xué)位級(jí)別】:碩士
【學(xué)位授予年份】:2015
【分類號(hào)】:Q51
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