摘要
Thethree-dimensional(3D)structurepredictionofproteinsisanimportanttaskinbioinformatics.Findingenergyfunctionsthatcanbetterrepresentresidue-residueandresidue-solventinteractionsisacrucialwaytoimprovethepredictionaccuracy.Thewidelyusedcontactenergyfunctionsmostlyonlyconsiderthecontactfrequencybetweendifferenttypesofresidues;however,wefindthatthecontactfrequencyalsorelatestotheresiduehydrophobicenvironment.Accordingly,wepresentanimprovedcontactenergyfunctiontointegratethetwofactors,whichcanreflecttheinfluenceofhydrophobicinteractiononthestabilizationofprotein3Dstructuremoreeffectively.Furthermore,afoldrecognition(threading)approachbasedonthisenergyfunctionisdeveloped.Thetestingresultsobtainedwith20randomlyselectedproteinsdemonstratethat,comparedwithcommoncontactenergyfunctions,theproposedenergyfunctioncanimprovetheaccuracyofthefoldtemplatepredictionfrom20%to50%,andcanalsoimprovetheaccuracyofthesequence-templatealignmentfrom35%to65%.
出版日期
2005年04月14日（中国期刊网平台首次上网日期，不代表论文的发表时间）
