Cotranslational Protein Folding and Terminus Hydrophobicity英文文献资料.docVIP

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Cotranslational Protein Folding and Terminus Hydrophobicity英文文献资料.doc

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Cotranslational Protein Folding and Terminus Hydrophobicity英文文献资料

HindawiPublishingCorporation AdvancesinBioinformatics Volume2011,ArticleID176813,8pages doi:10.1155/2011/176813 ResearchArticle CotranslationalProteinFoldingandTerminusHydrophobicity SheenalSrivastava,YumiPatton,DavidW.Fisher,andGrahamR.Wood DepartmentofStatistics,MacquarieUniversity,Sydney,NSW2109,Australia CorrespondenceshouldbeaddressedtoGrahamR.Wood,graham.wood@.au Received27December2010;Revised28February2011;Accepted24March2011 AcademicEditor:HuixiaoHong Copyright?2011SheenalSrivastavaetal.Thisis anopen accessarticle distributed under theCreative CommonsAttribution License,whichpermitsunrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalworkisproperly cited. Peptides fold on a time scale that is much smaller than the time required for synthesis, whence all proteins potentially fold cotranslationallytosomedegree(followedbyadditionalfoldingeventsafterreleasefromtheribosome).Inthispaper,inthree di?erentways,we?ndthatcotranslationalfoldingsuccessisassociatedwithhigherhydrophobicityattheN-terminusthanatthe C-terminus.First,wefoldsimpleHPmodelsonasquarelatticeandobservethatHPsequencesthatfoldbettercotranslationally thanfromafullyextendedstateexhibitapositivedi?erence(N?C)interminushydrophobicity.Second,weexaminerealproteins usingapreviouslyestablishedmeasureofpotentialcotranslationalityknownasALR(AverageLogarithmicRatiooftheextentof previouscontacts)andagain?ndacorrelationwiththedi?erenceinterminushydrophobicity.Finally,weusethecotranslational protein structure prediction programSAINTandagain?ndthatsuchanapproach tofoldingismoresuccessful forproteins withhigherN-terminusthanC-terminushydrophobicity.Allresultsindicatethatcotranslationalfoldingispromotedinpartbya hydrophobicstartandalesshydrophobic?nishtothesequence. 1.Background aproteinandhadthebraverytosuggestthatthismaybean indicatorofcotranslationalfolding.The?rst40residuesof theN-terminussequenceformsacompactglobularcorewith hydrophobicsidechains,whilethelast20residuesarefolded aro