The effect of phosphorylation on the conformation of oligo-peptides with Ser–Pro motif: a molecular dynamics simulation
The effect of phosphorylation on the conformation of oligo-peptides with Ser–Pro motif: a molecular dynamics simulation
复制标题
磷酸化对 Ser-Pro 基序寡肽构象的影响：分子动力学模拟
DOI：
10.1080/08927020601128904
复制
发表时间：
2007
影响因子：
2.1
通讯作者：
Yun
中科院分区：
文献类型：
--
作者：
Zhengqiaoruo Zhu;Yingfeng Li;Yan;Ming Sun;Yun
设计了四肽模型体系，研究了Ser-Pro基序肽基脯氨酰亚胺键的顺反异构化。为了建立侧链O-磷酸化在调节肽构象中的作用，通过MD Insight II Discovery 3方法对设计的四肽及其相应的磷酸化形式进行分子动力学（MD）模拟。最稳定的构型和统计的顺/反浓度分布表明，磷酸化明显影响的肽脯氨酰亚胺键异构化，并作为一个关键的影响，在调节肽的构象。电荷状态和提供给磷酸基团的电荷的位点可能是一个重要的关键。结果还表明，磷酸化改变了肽的顺式构象比例，当磷酸基团不带负电荷时，顺式构象比例最大。
Model tetrapeptide system was designed to investigate the cis/trans isomerization of peptidyl-prolyl imide bond of Ser–Pro motif. To establish the side-chain O-phosphorylation effect in regulating the peptides conformations, molecular dynamics (MD) simulations where carried out on the designed tetrapeptides and their corresponding phosphorylated forms by MD Insight II Discovery3 approach. The most stable configurations and the statistic cis/trans concentration distribution demonstrated that the phosphorylation evidently influences the peptidyl-prolyl imide bond isomerization and works as a key effect in regulating the peptide conformations. The charge state and the site provided for the charge of the phosphate moiety might be an important key. The results also demonstrated that phosphorylation changes the cis conformation ratio of the peptide and the maximum cis value is obtained when the phosphate group has no negative charge.
DOI：
10.1073/pnas.80.10.2926
发表时间：
1983-01-01
期刊：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子：
--
作者：
DAVIS, FM;TSAO, TY;RAO, PN
通讯作者：
RAO, PN