Multi-Scaled Explorations of Binding-Induced Folding of Intrinsically Disordered Protein Inhibitor IA3 to its Target Enzyme 英文参考文献.docVIP

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Multi-Scaled Explorations of Binding-Induced Folding of Intrinsically Disordered Protein Inhibitor IA3 to its Target Enzyme 英文参考文献.doc

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Multi-Scaled Explorations of Binding-Induced Folding of Intrinsically Disordered Protein Inhibitor IA3 to its Target Enzyme 英文参考文献

Multi-ScaledExplorationsofBinding-InducedFoldingof IntrinsicallyDisorderedProteinInhibitorIA3toitsTarget Enzyme JinWang1,2,3*,YongWang1,XiakunChu2,StephenJ.Hagen4,WeiHan2,ErkangWang1* 1StateKeyLaboratoryofElectroanalyticalChemistry,ChangchunInstituteofAppliedChemistry,ChineseAcademyofSciences,Changchun,Jilin,People’sRepublicof China,2CollegeofPhysics,JilinUniversity,Changchun,Jilin,People’sRepublicofChina,3DepartmentofChemistry,PhysicsandAppliedMathematics,StateUniversityof NewYorkatStonyBrook,StonyBrook,NewYork,UnitedStatesofAmerica,4DepartmentofPhysics,UniversityofFlorida,Gainesville,Florida,UnitedStatesofAmerica Abstract Biomolecularfunctionisrealizedbyrecognition,andincreasingevidenceshowsthatrecognitionisdeterminednotonlyby structure but also by flexibility and dynamics. We explored a biomolecular recognition process that involves a major conformational change – protein folding. In particular, we explore the binding-induced folding of IA3, an intrinsically disorderedproteinthatblockstheactivesitecleftoftheyeastasparticproteinasesaccharopepsin(YPrA)byfoldingitsown N-terminalresiduesintoanamphipathicalphahelix.Wedevelopedamulti-scaledapproachthatexplorestheunderlying mechanism by combining structure-based molecular dynamics simulations at the residue level with a stochastic path methodattheatomiclevel.Boththefreeenergyprofileandtheassociatedkineticpathsrevealacommonschemewhereby IA3bindstoitstargetenzymepriortofoldingitselfintoahelix.Thistheoreticalresultisconsistentwithrecenttime-resolved experiments.Furthermore,explorationofthedetailedtrajectoriesrevealstheimportantrolesofnon-nativeinteractionsin theinitialbindingthatoccurspriortoIA3folding.Incontrasttothecommonviewthatnon-nativeinteractionscontribute onlytotheroughnessoflandscapesandimpedebinding,thenon-nativeinteractionsherefacilitatebindingbyreducing significantlytheentropicsearchspaceinthelandscape.Theinformationgainedfrommulti-scaledsimulationsofthefolding ofthisintrinsicallydisorderedproteininthepresenc