新型室温熔盐二(三氟甲基磺酸酰)亚胺锂-乙酰胺体系的谱学研究

从分析二(三氟甲基磺酸酰)亚胺锂(LiTFSI)与乙酰胺形成熔盐的作用机制出发,通过红外和拉曼光谱的谱学分析并应用非局部密度泛函方法进行量化计算来对二者的相互作用进行了讨论.发现乙酰胺通过Li—O键与LiTFSI中Li+配位而破坏了LiTFSI的离子键,形成很大的配位阳离子,且正电荷被屏蔽在乙酰胺分子中;而TFSI-离子中电荷的部分离域导致电荷被终端—CF3基团屏蔽在整个分子中,这样两个大的阴阳离子间的库伦作用很弱;同时Li—O配位也导致乙酰胺分子间的氢键断裂,因而室温下体系以液体状态稳定存在.

Structure Exploration and Function Prediction of SARS Coronavirus E Protein

SARS E protein has long been taken only as membrane component of coronavirus. However, the researches have revealed that E proteins play an important multifunctional role in coronavirus virion life cycle. This investigation aims at exploring the three-dimensional(3D) structure of SARS E protein, especially for the loop region of its functional potential. As a result, a possible active site is found to be a cleavage in the C terminal, which is made up of nine amino acids. Additionally, the electrostatic property was employed to conform the possible active site. Electrostatic potential analysis prove that the active site really possesses the largest electrostatic property among the whole molecule domain, accordingly it will have a larger charge deposition and therefore may have stronger capabilities of interaction with possible ligand as well as other protein. The simulation results are helpful to providing insights into understanding the functions of SARS E protein and establishing molecular models for screening anti-SARS drug design.