分子伴侣GroE系统相互作用中结构与功能关系研究

根据大肠杆菌分子伴侣GroE系统的晶体结构数据，分析了GroEL顶端区域在其靶蛋白和GroES结合前后结构与功能的关系，讨论了GroEL的结构转变对其中心通道可及性和疏水特性的影响．提出了一种用以分析蛋白质之间相互作用趋势的方法，并用该方法分析了GroEL和GroES相互作用的3个氨基酸，得到了很好的结果。在此基础上，进一步用SwissPDBViewer对GroEL的核酸结合口袋进行了分析，结果表明活性中心与ADP磷酸键结合的残基Thr30可能与能量的传递有关．

Research on the Relation of Structure and Function of Molecular Chaperone GroE

Based upon the crystal structural data from PDB, The relation of structure and function of GroEL apical domain combined with GroES and target protein or not, is studied, as well as the influence of the structural changes of GroEL on the accessibility and the hydrophobicity of its central cavity. Put forward a new method to analyze the interaction propensity of proteins. Using this method, we analyze the three amino acids at the interaction surface of GroEL and GroES and acquire a good result. The nucleotide-binding pocket of GroEL equatorial domain is further analyzed using SwissPDBViewer. The result shows that the residue Thr30 located in the active center which binds to one phosphate group of ADP may be involved in the energy transferring.