简介：Proteinphosphorylationplaysanimportantroleinvariouscellularprocesses.Duetoitshighcomplexity,themechanismneedstobefurtherstudied.Inthelastfewyears,manymethodshavebeencontributedtothisfield,butalmostalloftheminvestigatedthemechanismbasedonproteinsequencesaroundproteinsites.Inthisstudy,weimplementanexplorationbycharacterizingthemicroenvironmentsurroundingphosphorylatedproteinsiteswithamodifiedshellmodel,andobtainsomesignificantpropertiesbytherank-sumtest,suchasthelackofsomeclassesofresidues,atoms,andsecondarystructures.Furthermore,wefindthatthedepletionofsomepropertiesaffectsproteinphosphorylationremarkably.Ourresultssuggestthatitisameaningfuldirectiontoexplorethemechanismofproteinphosphorylationfrommicroenvironmentandweexpectfurtherfindingsalongwiththeincreasingsizeofphosphorylationandproteinstructuredata.

简介：Phosphorylatedmesoporouscarbons(PMCs)wereinvestigatedascatalystsinthedehydrationoffructosetohydroxymethylfurfural(HMF).TheacidicPMCsshowbetterselectivitytoHMFcomparedtosulfonatedcarboncatalyst(SC)despiteloweractivity.TheconcentrationofP-OgroupsonthePMCwascorrelatedwiththeactivity/selectivityofthecatalysts;thehighertheP-Oconcentration,thehighertheactivity.However,thehighertheP-Ocontent,thelowertheselectivitytoHMF.Indeed,alowerconcentrationoftheP-OgroupsminimizedthedegradationofHMFtolevulinicacidandtheformationofby-products,suchashumines.Stabilitytestsshowedthatthesesystemsdeactivateduetotheformationofhuminesandwaterinsolubleby-productsderivedfromthedehydrationoffructosewhichblockedthecatalyticallyactivesites.

简介：ThelaserphotolysisofN-diisopropylphosphoryltryptophyltyrosinedipeptidemethylester(N-DiPP-TrpH-TyrOH)hasbeencarriedoututilizingaKrF(248nm)laser.ThedirectintramolecularETbetweenTrpH+residueandTyrOHresiduewasdetectedfirstandtheETbetweenTrpandTyrOHbecameslow.Itwassuggestedthatphosphorylgroupstabilizeneighbourradicalofaromaticringbyhyperconjugation.IncombinationwithcomputermodelingweobtainedthekineticparametersoftheETandprovedthatphosphorylgroupstookpartintheprocessofET.Theresultsshouldbesignificantforbiologicalsystemsinceeverybiologicalprocessinvolvesthephosphorylationornonphosphorylation.