.png){kind=icon}
返回
How Cations Change Peptide Structure
.png){kind=icon}
OA
AI
DOI：10.1002/chem.201204554.png)
.png){kind=icon}
原文求助.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
Abstract Specific interactions between cations and proteins have a strong impact on peptide and protein structure. Herein, we shed light on the nature of the underlying interactions, especially regarding effects on the polyamide backbone structure. This was done by comparing the conformational ensembles of model peptides in isolation and in the presence of either Li+ or Na+ by using state-of-the-art density-functional theory (including van der Waals effects) and gas-phase infrared spectroscopy. These monovalent cations have a drastic effect on the local backbone conformation of turn-forming peptides, by disruption of the hydrogen-bonding networks, thus resulting in severe distortion of the backbone conformations. In fact, Li+ and Na+ can even have different conformational effects on the same peptide. We also assess the predictive power of current approximate density functionals for peptide-cation systems and compare to results with those of established protein force fields as well as high-level quantum chemistry calculations (CCSD(T)).
Keyword:
density-functional calculations
hydrogen bonds
IR spectroscopy
protein folding
protein structures
期刊
C
IF:
3.7
论文数:
3.9W
被引数:
9.6W
机构
引用论文
Polyaniline-modified activated carbon electrodes for capacitive deionisation用于电容去离子的聚苯胺改性活性炭电极.png)
Desalination
DesalinationIF0
PREAI
分享收藏Comparative study of GeO2/Ge and SiO2/Si structures on anomalous charging of oxide films upon water adsorption revealed by ambient-pressure X-ray photoelectron spectroscopy通过环境压力x射线光电子能谱揭示的GeO2/Ge和SiO2/Si结构对水吸附后氧化膜异常充电的比较研究OAAI
OAAI分享收藏
查看更多内容