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Science China(Physics,Mechanics & Astronomy) 2005年第5期48卷 585-592页

作者： WANG Weining1, YAN Haitao1, YUE Weiwei1, ZHAO Guozhong1, ZHANG Cunlin1, LIU Haibo2 & ZHANG Xicheng2 1. Department of Physics, Capital Normal University, Beijing 100037, China 2. Center for Terahertz Research, Rensselaer Polytechnic Institute, Tory, NY, USA Department of Physics Capital Normal Univesity Beijing China Center for Terahertz Research Rensselaer Polytechnic Institute Tory USA

The optical characteristics of reduced glutathione molecules between 0.2 THz and 2.4 THz have been investigated by THz time-domain spectroscopy (THz-TDS). The absorption characteristics and optical parameters of the reduced glutathione purged with Nitrogen at room temperature were obtained experimentally. The measured results were fitted well with the theoretical results computed by using Density Functional Theory (DFT) in far-infrared range. Also the conformation of the reduced glutathione molecule was simulated by Gaussian 03. This work has demonstrated significantly that THz-TDS spectroscopy can further be used to study other biological molecules in biological and biomedical engineering.

关键词： THz time domain spectroscopy, reduced glutathione, absorption spectrum, biological engineering.

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Molecular dynamics simulation study on zwitterionic structure to maintain the normal conformations of glutathione

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Science China Chemistry 2007年第5期50卷 660-664页

作者： YAN Han1, ZHU HaoMiao2 & SHEN Jian1,2 1 Jiangsu Research Center of Surface and Interface Chemical Engineering and Technology, Nanjing University, Nanjing 210093, China 2 Jiangsu Engineering Research Center for Bio-medical function Materials, Nanjing Normal University, Nanjing 210097, China Jiangsu Research Center of Surface and Interface Chemical Engineering and Technology Nanjing University Nanjing China Jiangsu Engineering Research Center for Bio-medical function Materials Nanjing Normal University Nanjing China

Molecular dynamics simulations were applied to normal conformational glutathione (GSH) and GSH over zwitterionic and hydrophobic surfaces respectively. Conformational analysis of GSH during the simulation time on RMSD, conformational flexibility and dihedral distribution were performed. The re- sults showed that zwitterionic structure maintains the normal conformations of GSH to a better extent, which should be a first good proof of the hypothesis of "maintain of normal structure".

关键词： protein-surface interactions, molecular dynamics simulation, zwitterionic structure, glutathione, conformational changes, antithrombotic material

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