蛋白质-rna基于氨基酸序列的无序性和磷酸化研究及亲和力常数数据集的构建word论文.docxVIP

AbstractIntrinsically disordered proteins are a new class of proteins which lack unique tertiary structures under native conditions，but they are biologically active. It extends the protein “sequence-structure-function” paradigm. Intrinsically disordered protein is anensemble of a variety of coexisting conformations and constantly dynamic changes under native conditons. Therefore they play important roles in the cell, such as signal, recognition and regulation. Deep studies of intrinsically protein will promote people a better understanding of the relationship between protein structure and function.Comparing to protein-protein interaction and protein-DNA interaction ,there are less relevance research between protein disorder region and function on protein-RNA interaction. Our work is divided into two parts. Firstly, we analyzed the disorder sites and the correlation between disordered and phosphorylation sites in RNA-binding proteins in the human genome. Results show that the disordered residues/tails content in the RNA-binding protein is higher, and 57.52% of RNA-binding protein phosphorylation sites is located in a disordered residue, similar with DNA binding protein, higher than the non RNA binding proteins. Secondly, we study the coupling effect of disorder and phosphorylation on protein-RNA interaction. Disordered residues tend to be located at any area in addition to protein-RNA binding interface. Phosphorylation site tend to be located at protein-RNA binding interface. And phosphorylation site and disordered site is not coupled.Also, we developed a non-redundant protein-RNA binding benchmark dataset derived from the Protein Database Bank. It consists of 73 complexes with measured binding affinity. This dataset will be helpful for the research on protein-RNA docking and binding mechanism.Key words: Intrinsically disordered proteins; RNA-binding proteins; phosphorylatio nbinding affinity; correlation目 录摘要 .......................................................