Analysis Of Intrinsically Disordered And Phosphorylation Based On Amino Acid Sequence In Protein-RNA And Dataset Construction Of Binding Affinity

Intrinsically disordered proteins are a new class of proteins which lack uniquetertiary structures under native conditions，but they are biologically active. It extends theprotein “sequence-structure-function” paradigm. Intrinsically disordered protein is anensemble of a variety of coexisting conformations and constantly dynamic changes undernative conditons. Therefore they play important roles in the cell, such as signal,recognition and regulation. Deep studies of intrinsically protein will promote people abetter understanding of the relationship between protein structure and function.Comparing to protein-protein interaction and protein-DNA interaction,there are lessrelevance research between protein disorder region and function on protein-RNAinteraction. Our work is divided into two parts. Firstly, we analyzed the disorder sites andthe correlation between disordered and phosphorylation sites in RNA-binding proteins inthe human genome. Results show that the disordered residues/tails content in the RNA-binding protein is higher, and57.52%of RNA-binding protein phosphorylation sites islocated in a disordered residue, similar with DNA binding protein, higher than the nonRNA binding proteins. Secondly, we study the coupling effect of disorder andphosphorylation on protein-RNA interaction. Disordered residues tend to be located atany area in addition to protein-RNA binding interface. Phosphorylation site tend to belocated at protein-RNA binding interface. And phosphorylation site and disordered site isnot coupled.Also, we developed a non-redundant protein-RNA binding benchmark datasetderived from the Protein Database Bank. It consists of73complexes with measuredbinding affinity. This dataset will be helpful for the research on protein-RNA dockingand binding mechanism.