Renaturation of soluble and immobilized ribonuclease: are the polypeptide folding pathways for structure formation the same for soluble proteins and for proteins associated with a surface?

Journal of applied biochemistry Pub Date : 1985-02-01
V G Janolino, H E Swaisgood, H R Horton
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Abstract

During the refolding and oxidation of reductively denatured ribonuclease A in solution, there is a marked lag in appearance of enzymatic activity as compared to the oxidation of sulfhydryl groups, whether such oxidation is spontaneous or is catalyzed by sulfhydryl oxidase. However, if ribonuclease is covalently attached to a derivatized glass surface, a lag period is not observed during the reformation of native structure from the completely reduced, denatured state. These results suggest that, in solution, intermolecular interactions alter the pathway of polypeptide chain folding and disulfide bond formation, leading to nonnative disulfides which do not rapidly interchange to form native pairings. The isolation of refolding polypeptide chains by covalent immobilization prevents such interactions. Presumably, such intermolecular interactions would be similarly prevented by "isolation" of nascent polypeptide chains during protein synthesis on ribosomes.

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可溶性核糖核酸酶和固定化核糖核酸酶的再生:结构形成的多肽折叠途径对于可溶性蛋白质和与表面相关的蛋白质是相同的吗?
在溶液中还原变性核糖核酸酶A的再折叠和氧化过程中,与巯基的氧化相比,酶活性的表现明显滞后,无论这种氧化是自发的还是由巯基氧化酶催化的。然而,如果核糖核酸酶共价附着在衍生化的玻璃表面,则在从完全还原,变性状态的天然结构的改造过程中不会观察到滞后期。这些结果表明,在溶液中,分子间相互作用改变了多肽链折叠和二硫键形成的途径,导致非天然二硫化物不能迅速交换形成天然配对。通过共价固定分离重折叠多肽链可以防止这种相互作用。据推测,在核糖体上合成蛋白质的过程中,新生多肽链的“隔离”同样会阻止这种分子间的相互作用。
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