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

  • Zuoyin Yang
  • Zongchao Jia
  • Ruozhuang Liu
  • Guangju Chen


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 monomerś 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.


antifreeze protein recognition dynamics simulation molecular mechanics quantum chemistry 


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Copyright information

© Science in China Press 2004

Authors and Affiliations

  • Zuoyin Yang
    • 1
    • 2
  • Zongchao Jia
    • 3
  • Ruozhuang Liu
    • 1
  • Guangju Chen
    • 1
  1. 1.Department of ChemistryBeijing Normal UniversityBeijingChina
  2. 2.Faculty of Science, Beijing University of Chemical TechnologyBeijingChina
  3. 3.Department of BiochemistryQueenś UniversityKingstonCanada

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