的反应性，从而构成细胞内巯基库的一部分来调控细胞内的氧化还原电位。
effectsofmolecularchaperones,proteinaggregationandmacromolecularcrowdingonproteinfolding
“halfofthesites”bindingofd-glyceraldehyde-3-phohatedehydrogenasefoldingintermediatewithgroel.twod-glyceraldehyde-3-phohatedehydrogenase(gapdh)foldingintermediatesubunitsbindwithgroeltoformastablecomplex,whichcannolongerbindwithadditionalgapdhintermediatesubunits,butdoesbindwithonemorelysozymefoldingintermediateoronegroesmolecule,suggestingthatthetwogapdhsubunitsbindatoneendofthegroelmoleculedilayinga“halfofthesites”bindingprofile.forlysozyme,groelbindswitheitheroneortwofoldingintermediatestoformastable1:1or1:2complexwithonesutrateoneachendofthegroeldoubleringforthelatter.the1:1complexof(groel-groes)bindswithonelysozymeoronedimer

icgapdhfoldingintermediatetoformastableternarycomplex.bothcomplexesof(groel-lysozyme1)and(groel-gapdh2)bindwithonegroesmoleculeonlyattheotherendofthegroelmoleculeformingatraternarycomplex.accordingtothestoichiometryofgroelbindingwiththegapdhfoldingintermediateandtheformationofternarycomplexescontaininggroel-gapdh2,itissuggestedthatthefoldingintermediateofgapdhbinds,verylikelyinthedimericform,withgroelatoneendonly.
aggregatedproteiacceleratebutdonotincreasetheaggregationofd-glyceraldehyde-3-phohatedehydrogenase.ecificityofproteinaggregation.theeffectofproteinaggregatesontheaggregationofgapdhduringunfoldingandrefoldinghasbeenstudied.theaggregationofgapdhfollowsasigmoidcourse.thepresenceofproteinaggregatesincreases

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