Dissection of the Zipping-and-Assembly Mechanism for Folding of Model Proteins  被引量:2

Dissection of the Zipping-and-Assembly Mechanism for Folding of Model Proteins

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作  者:孙理 王骏 王炜 

机构地区:[1]Nanjing National Laboratory of Microstructure and Department of Physics, Nanjing University, Nanjing 210093

出  处:《Chinese Physics Letters》2010年第3期332-335,共4页中国物理快报(英文版)

基  金:Supported by the National Basic Research Program under Grant Nos 2006CB910302 and 2007CB814806, the National Natural Science Foundation under Grant Nos 10834002 and 10774069, the Foundation for the Author of National Excellent Doctoral Dissertation of China, and the Fund of Jiangsu Province (BK2009008).

摘  要:Zipping-and-assembly mechanism (ZAM) is a new mechanism describing the kinetics of protein folding. To dissect the validity of this mechanism for various protein-like systems, a prediction test based on three-dimensional HP lattice models is carried out. It is found that only the native structures of a part of protein-like models could be predicted with a ZAM-based method. The detailed comparisons between the model proteins which are predicted or failed with the ZAM-based method suggest that the ZAM is likely to be applicable for the model proteins with the weak hydrophobicity, the low contact order for native conformations, and the large separation between the energies of native state and denatured states. These observations bring us more information about the protein-like systems for which the ZAM could be applied.Zipping-and-assembly mechanism (ZAM) is a new mechanism describing the kinetics of protein folding. To dissect the validity of this mechanism for various protein-like systems, a prediction test based on three-dimensional HP lattice models is carried out. It is found that only the native structures of a part of protein-like models could be predicted with a ZAM-based method. The detailed comparisons between the model proteins which are predicted or failed with the ZAM-based method suggest that the ZAM is likely to be applicable for the model proteins with the weak hydrophobicity, the low contact order for native conformations, and the large separation between the energies of native state and denatured states. These observations bring us more information about the protein-like systems for which the ZAM could be applied.

关 键 词:Biological physics 

分 类 号:Q51[生物学—生物化学] TM923.64[电气工程—电力电子与电力传动]

 

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