Binding Models of Antifreeze Protein Surfaces into Ice Faces
Antifreeze protein (AFP) can protect organisms from damage in freezing conditions by controlling ice growth (thermal hysteresis activity) and inhibiting recrystallization of ice granules (recrystallization inhibition activity) respectively. Formerly, hydrogen-bonding matching model was used to explain the surface binding mechanism between AFPs and ices, however, it is only suitable for one or several AFPs, but not for the others. Therefore, basing on the newly developed mode of surface complementarity, we used bioinformatics methods, especially protein docking, to obtain the molecular models of AFPs and hence to interpret the molecular mechanism. Relatively perfect molecular models of surface complementarity were obtained according to solved or modeled three-dimensional structures of all discovered AFPs, including fish AFPs, insect AFPs and plant AFPs, revealing a underlying element for molecular mechanisms. Among the forces of models of surface complementarity, van der waals force and hydrophobic interaction is the key roles, but hydrogen bond is subsidiary.
Antifreeze protein Ice faces Surface complementarity Protein docking Bioinformatics
Dang-Quan Zhang Xiao-Feng Tan Wan-Xi Peng Qi-Mei Liu Yan-Ling Zeng Hong-Peng Chen
The Key Lab of Non-Wood Forest Products of State Forestry Administration, Central South University o Institute of Rheology Mechanics and Material Engineering, CSUFT, Changsha 410004, China
国际会议
The 5th International Forum on Post-genome Technologies(5IFPT)(第五届国际后基因组生命科学技术学术论坛)
苏州
英文
2007-09-10（万方平台首次上网日期，不代表论文的发表时间）