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1、ViewOnline/JournalHomepage/TableofContentsforthisissuePCCPDynamicArticleLinksCitethis:Phys.Chem.Chem.Phys.,2012,14,415–426www.rsc.org/pccpPERSPECTIVEHowionicliquidscanhelptostabilizenativeproteinsabcHermannWeinga¨rtner,*ChiaraCabreleandChristianHerrmannReceived15thJune2011,Accepted
2、26thOctober2011DOI:10.1039/c1cp21947bThenativestateofaglobularproteinisessentialforitsbiocatalyticfunction,butismarginallystableagainstunfolding.Whileunfoldingequilibriaareoftenreversible,foldingintermediatesandmisfoldscanpromoteirreversibleproteinaggregationintoamorphousprecipitat
3、esorhighlyorderedamyloidstates.Additionofionicliquids—low-meltingorganicsalts—offersintriguingprospectsforstabilizingnativeproteinsandtheirenzymaticfunctionagainstthesedeactivatingreactionchannels.Thehugenumberofcationsandanionsthatformionicliquidsallowsfine-tuningoftheirsolventprope
4、rties,whichoffersrobustandefficientstrategiesforsolventoptimization.Goingbeyondcase-by-casestudies,thisarticleaimsatdiscussingprinciplesforarationaldesignofionicliquid-basedformulationsinproteinchemistryandbiocatalysis.Introductiontotheenergyofthreehydrogenbonds.Forcomparison,heneggwh
5、itelysozyme—anoftenusedprotein—containsaboutProteinsfoldtoanativestructure,whichisessentialfortheirtwohundredintrapeptideH-bonds.enzymaticfunction.Despitetheirmoleculardiversity,nativeThelowstabilityreflectsasubtlebalanceofmolecular1proteinssharethecommontraitofbeingonlymarginallyst
6、able.forces.StabilizationprimarilyresultsfromhydrophobicforcesTheGibbsenergyofunfoldingfromthenativestateNtoanandH-bonds,whiledestabilizationismainlyfoundedinensembleofunfoldedstatesU,DunfG=GUGN,istypicallyanentropicforceduetothelossofconfigurationalfreedom2lessthan60kJpermolofprot
7、ein,whichroughlycorrespondsofthefoldedchain.1Itneedsonlyamoderateenvironmental23DownloadedbyHenanNormalUniversityon15May2012stress,suchasanincreaseintemperatureorpressureorthe4,5aadditionofaco-solvent,toupsetthisbalance.Forexample,DepartmentofPhysicalChemistryII,FacultyofChemistrya
8、ndPublishedon16November201
