简介：Theexactstructureofanarginine-carboxylatesaltbridgeindifferentchemicalenvironmentsremainsacontroversialproblem.Inthepresentwork,thezwitterionicandneutralformsofarginine-carboxylatesaltbridgewerestudiedbytheB3LYP/6-311G(d,p)//PM3method.Itturnsoutthattheneutralformsaremorestablethanthezwitterioniccoumterpartsingasphase.However,whnenboundbyα-cyclodextrin,thezwitterionicformsbecomemorestablethanthecorrespondingneutralones.Itissuggestedthatthehydrophobicenvironmentprovidedbythecyclodextrincavityleadstosuchbehavior.Therefore,thesaltbridgestillcouldbeinazwitterionicforminthehydrophobicinterioroftherealproteins.
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