Prediction and Dissection of Widely-Varying Association Rate Constants of Actin-Binding Proteins 英文参考文献.docVIP

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Prediction and Dissection of Widely-Varying Association Rate Constants of Actin-Binding Proteins 英文参考文献.doc

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Prediction and Dissection of Widely-Varying Association Rate Constants of Actin-Binding Proteins 英文参考文献

PredictionandDissectionofWidely-VaryingAssociation RateConstantsofActin-BindingProteins XiaodongPang1.,KennethH.Zhou2.,SanboQin1,Huan-XiangZhou1* 1Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, United States of America, 2Lawton Chiles High School, Tallahassee,Florida,UnitedStatesofAmerica Abstract Actin is an abundant protein that constitutes a main component of the eukaryotic cytoskeleton. Its polymerization and depolymerization are regulated by a variety of actin-binding proteins. Their functions range from nucleation of actin polymerization to sequestering G-actin in 1:1 complexes. The kinetics of forming these complexes, with rate constants varyingatleastthreeordersofmagnitude,iscriticaltothedistinctregulatoryfunctions.Previouslywehavedevelopeda transient-complex theory for computing protein association mechanisms and association rate constants. The transient complex refers to an intermediate in which the two associating proteins have near-native separation and relative orientationbuthaveyettoformshort-rangespecificinteractionsofthenativecomplex.Theassociationrateconstantis predictedaska=ka0e{DGel?=kBT,whereka0isthebasalrateconstantforreachingthetransientcomplexbyfreediffusion, andtheBoltzmannfactorcapturesthebiasoflong-rangeelectrostaticinteractions.Hereweappliedthetransient-complex theorytostudytheassociationkineticsofsevenactin-bindingproteinswithG-actin.Theseproteinsexhibitthreeclassesof associationmechanisms,duetotheirdifferentmolecularshapesandflexibility.The1000-foldkavariationsamongthemcan mostlybeattributedtodisparateelectrostaticcontributions.Thebasalrateconstantsalsoshowedvariations,resultingfrom the different shapes and sizes of the interfaces formed by the seven actin-binding proteins with G-actin. This study demonstrates the various ways that actin-binding proteins usephysical properties totune their association mechanisms andrateconstantstosuitdistinctregulatoryfunctions. Citation: Pa