小窩蛋白-1在不對稱雙層膜模型中的動力學行為研究
發(fā)布時間：2018-12-19 21:37
【摘要】：小窩是細胞膜上富含鞘脂類和膽固醇的不對稱雙層膜結(jié)構(gòu),廣泛參與信號傳導、胞吞作用、脂類運輸?shù)榷喾N生物進程。小窩蛋白是小窩的基本組成蛋白,小窩蛋白的功能障礙和錯誤調(diào)節(jié)與很多重大疾病的發(fā)生相關(guān),因此對小窩蛋白的研究具有重大意義。但是小窩蛋白的結(jié)構(gòu)尚未被解析,其在小窩中的構(gòu)象也不清楚。小窩蛋白-1是最早被發(fā)現(xiàn)也是分布最廣的小窩蛋白亞型,同時也是一個膽固醇結(jié)合蛋白。本論文主要對小窩蛋白-1在不對稱磷脂雙分子膜中的動力學行為進行研究。為了模擬真實的小窩膜環(huán)境,論文第二章主要搭建了內(nèi)外膜中磷脂成分不一樣的雙層膜模型,對該模型的分子動力學模擬證實了模型的穩(wěn)定性。論文第三章在第二章的基礎上搭建了小窩蛋白-1(殘基82-136)和不對稱雙層膜模型的復合體系,通過兩條1微秒的分子動力學模擬,我們發(fā)現(xiàn)小窩蛋白-1的腳手架區(qū)域(殘基82-101)能與跨膜區(qū)的一部分(殘基102-107)一起形成一個完整的a-螺旋結(jié)構(gòu),小窩蛋白-1(殘基82-136)能以“U”形構(gòu)象在膜中穩(wěn)定存在。在模擬中,小窩蛋白-1(殘基82-136)僅插入不對稱雙層膜的內(nèi)膜,能夠增加內(nèi)膜磷脂分子的有序性而降低外膜磷脂分子的有序性。另外,在小窩蛋白-1的腳手架區(qū)域沒有發(fā)現(xiàn)膽固醇的傾向性結(jié)合位點。
[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.
【學位授予單位】：華東理工大學
【學位級別】：碩士
【學位授予年份】：2015
【分類號】：Q51
本文編號：2387501
[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.
【學位授予單位】：華東理工大學
【學位級別】：碩士
【學位授予年份】：2015
【分類號】：Q51
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