|本期目录/Table of Contents|

锌指蛋白去折叠的全原子模拟(PDF)

《内蒙古大学学报(自然科学版)》[ISSN:1000-9035/CN:22-1262/O4]

期数:
2019年06期
页码:
631-636
栏目:
研究论文
出版日期:
2019-11-15

文章信息/Info

Title:
Atomistic Unfolding Simulation of Zn-finger Proteins
作者:
和二斌12罗志荣1
1.玉林师范学院物理与电信工程学院,广西 玉林 537000; 2.玉林师范学院广西高校复杂系统优化与大数据处理重点实验室,广西 玉林 537000
Author(s):
HE Er-bin12LUO Zhi-rong1
1.School of Physics and Telecommunications Engineering,Yulin Normal University,Yulin 537000,China;
2.Guangxi Universities Key Lab of Complex System Optimization and Big Data Processing,Yulin Normal University,Yulin 537000,China
关键词:
锌指 去折叠 锌离子 动力学模拟
Keywords:
zinc finger unfolding zinc ion dynamics simulation
分类号:
-
DOI:
-
文献标识码:
A
摘要:
锌指蛋白是一种广泛存在于真核细胞的转录蛋白,在生命过程中扮演着重要作用,通过锌离子与特定残基的绑定来维持结构的稳定.作为一种重要的功能结构,锌指蛋白为研究锌离子参与的蛋白质折叠/去折叠问题提供了一个极好的模型.对锌指蛋白去折叠过程进行了原子层次的统计分析.研究发现,锌离子不仅能够稳定蛋白质的天然结构,而且参与了整个去折叠过程; 此外,也发现Trp7在残基解离次序方面起着重要的作用.在去折叠的过程中,水分子与去折叠过程的耦合关系表现为驱逐机制.该研究也揭示了金属离子相关蛋白质去折叠过程的一般机制.
Abstract:
As a transcriptional protein,zinc-finger proteins widely exist in eukaryotic cells and play crucial roles in life processes,and depen on the binding of zinc ions with special residues for their structure stability.As an important functional structure,zinc finger proteins provide an excellent model for studying the roles of zinc ions in the folding/unfolding process.Here an atomistic and statistical analysis of the unfolding of the zinc finger proteins is given.The results show that zinc ions not only stabilize the native structure but also participate in the whole unfolding process.It is also found that the hydrophobic residue Trp7 plays an essential role in the unbinding order.Water molecules are found to be coupled with the unfolding process via the expulsion mechanism.The results provide significant insight into the general mechanisms of the metal cofactor dependent protein-unfolding.

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备注/Memo

备注/Memo:
收稿日期:2019-01-24; 修回日期:2019-03-21
基金项目:国家自然科学基金项目(51561031); 玉林师范学院高层次人才科研启动项目(G2017005)
作者简介:和二斌(1980-),男,河南焦作人,讲师,博士.E-mail:herbin@live.cn
更新日期/Last Update: