theaggregationrateduringunfoldingandrefoldingofgapdh,butdidnotchangetheextentofaggregationandthefinalrenaturationyield.itissuggestedthatproteinaggregatesfunctionasseedsforaggregationviahydrophobicinteractionwithonlygapdhfoldingintermediatesdestinedtoaggregateanddonotaffectthedistributionbetweenpathwaysleadingtocorrectfoldingandaggregation.moreover,twodifferentproteidonotinterferewitheachotherduringtheirsimultaneousrefoldingtogetherinabuffer.thesefindingsprovideiightsintoamechanismbywhichcellspreventproteinfoldingagaitinterferencefromaggregationofotherprotei.
onlythereducedconformerofa-lactalbuminisinducibletoaggregationbyproteinaggregates.reducedapo-a-lactalbumin(r-la)inpre-moltenglobulestateissolubleinneutralandreducedbufferat25ocbutbecomesaggregatedwhenaggregatesofvariousproteiareadded.however,proteinaggregatesdonotinducetheaggregationofapo-a-lactalbumininthemoltenglobulestate.thepresenceofmolecularchaperone,proteindisulfideisomerase(pdi),orthe“chemicalchaperone”,polyethyleneglycol,inhibitstheinducedaggregation.nativeprotei,aggregation-freefoldingintermediatesandsolubleaggregatesdonotinducetheaggregation.theinteractionbetweenr-laandproteinaggregatesishydrophobicinnature.thesefindingsuggestthatpre-moltenglobulestateoflaisthetargetnotonlyforchaperonesbu
talsoforproteinaggregates.
effectsofmacromolecularcrowdingontherefoldingofglucose-6-phohatedehydrogenaseandproteindisulfideisomerase.intracellularenvironmentisactuallycrowdedorconfined.theeffectsofhighconcentra
上一页 [1] [2] [3] [4] [5] [6] 下一页