Dynamic consequences of mutating the typical HPGG motif of apocytochrome b_5 revealed by computer simulation |
| |
| Authors: | Ying Wu Lin Tian Lei Yingc Li Fu Liaoa a School of Chemistry Chemical Engineering University of South China Hengyang China b |
| |
| Affiliation: | a School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China;b Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA;c Chemical Biology Lab, Department of Chemistry, Fudan University, Shanghai 200433, China |
| |
| Abstract: | Apecytochrome b5 with a typical heme-binding motif of HPGC,and its variants with mutated motifs,GPGG,GPGH,HVGG,and HPGP,have been subjected to molecular dynamics simulation.Comparison of the dynamic consequences has revealed the crucial role of HPGG in assembling the heme group of cytochrome b5 and in modulating protein structure,property and function. |
| |
| Keywords: | Apocytochrome b5 Heme-binding motif HPGC Molecular dynamics simulation |
| 本文献已被 CNKI 维普 万方数据 ScienceDirect 等数据库收录！ |
| 点击此处可从《中国化学快报》浏览原始摘要信息 |
|
点击此处可从《中国化学快报》下载全文 |
|
