Molecular and quantum mechanical studies on the monomer recognition of a highly-regular β-helical antifreeze protein  

作　　者：YANG Zuoyin, JIA Zongchao, LIU Ruozhuang & CHEN GuangjuDepartment of Chemistry, Beijing Normal University, Beijing 100875, China Faculty of Science, Beijing University of Chemical Technology, Beijing 100029, China Department of Biochemistry, Queen’s University, Kingston, Ontario K7L 3N6, Canada 

出　　处：《Science China Chemistry》2004年第1期34-40,共7页中国科学（化学英文版）

基　　金：This work was supported by the National Natural Science Foundation of China(Grant Nos.20271009,20231010,30228006 and 29992590-1);the Major State Basic Research Development Programs(Grant No.G2000078100);the Foundation for Key Projection and SRF for ROCS by the Ministry of Education of China.

摘　　要：The possible interaction models for an antifreeze protein from Tenebrio molitar (TmAFP) have been systematically studied using the methods of molecular mechanics, molecular dynamics and quantum chemistry. It is hoped that these approaches would provide insights into the nature of interaction between protein monomers through sampling a number of interaction possibilities and evaluating their interaction energies between two monomers in the course of recognition. The results derived from the molecular mechanics indicate that monomer? β-sheets would be involved in interaction area and the side chains on two p-faces can match each other at the two-dimensional level. The results from molecular mechanics and ONIOM methods show that the strongest interaction energy could be gained through the formation of H-bonds when the twoβ-sheets are involved in the interaction model. Furthermore, the calculation of DFT and analysis of van der Waals bond charge density confirm further that recognition between the two TCTs mainly depends on inter-molecular hydroxyls. Therefore, our results demonstrate that during the course of interaction the most favorable association of TmAFPs is via their β-sheets.The possible interaction models for an antifreeze protein from Tenebrio molitar (TmAFP) have been systematically studied using the methods of molecular mechanics, molecular dynamics and quantum chemistry. It is hoped that these approaches would provide insights into the nature of interaction between protein monomers through sampling a number of interaction possibilities and evaluating their interaction energies between two monomers in the course of recognition. The results derived from the molecular mechanics indicate that monomer's β-sheets would be involved in interaction area and the side chains on two β-faces can match each other at the two-dimensional level. The results from molecular mechanics and ONIOM methods show that the strongest interaction energy could be gained through the formation of H-bonds when the two β-sheets are involved in the interaction model. Furthermore, the calculation of DFT and analysis of van der Waals bond charge density confirm further that recognition between the two TCTs mainly depends on inter-molecular hydroxyls. Therefore, our results demonstrate that during the course of interaction the most favorable association of TmAFPs is via their β-sheets.

关 键 词：ANTIFREEZE protein  recognition  dynamics simulation  MOLECULAR mechanics  quantum chemistry. 

分 类 号：O621.13[理学—有机化学]