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Influence of the internal disulfide bridge on the folding pathway of the C-L antibody domain

机译：内部二硫键对C-L抗体结构域折叠途径的影响

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摘要

Disulfide bridges are one of the most important factors stabilizing the native structure of a protein. Whereas the basis for their stabilizing effect is well understood, their role in a protein folding reaction still seems to require further attention. We used the constant domain of the antibody fight chain (CL), a representative of the ubiquitous immunoglobulin (Ig)-superfamily, to delineate the kinetic role of its single buried disulfide bridge. Independent of its redox state, the monomeric CL domain adopts a typical Ig-fold under native conditions and does not retain significant structural elements when unfolded. Interestingly, its folding pathway is strongly influenced by the disulfide bridge. The more stable oxidized protein folds via a highly structured on-pathway intermediate, whereas the destabilized reduced protein populates a misfolded off-pathway species on its way to the native state. In both cases, the formation of the intermediate species is shown to be independent of the isomerization. state of the Tyr(141)-Pro(142) bond. Our results demonstrate that the internal disulfide bridge in an antibody domain restricts the folding pathway by bringing residues of the folding nucleus into proximity thus facilitating the way to the native state. (c) 2006 Elsevier Ltd. All rights reserved.
机译：二硫键是稳定蛋白质天然结构的最重要因素之一。尽管已经很好地了解了其稳定作用的基础，但它们在蛋白质折叠反应中的作用似乎仍需进一步关注。我们使用了抗体战斗链（CL）的恒定域（普遍存在的免疫球蛋白（Ig）-超家族的代表）来描述其单个掩埋的二硫键的动力学作用。不依赖于其氧化还原状态，单体CL结构域在天然条件下采用典型的Ig折叠，并且在展开时不会保留重要的结构元素。有趣的是，其折叠途径受到二硫键的强烈影响。较稳定的氧化蛋白通过高度结构化的途中中间体折叠，而不稳定的还原蛋白则在其向天然状态的途中填充了错误折叠的偏向物种。在两种情况下，中间体种类的形成均与异构化无关。 （141）-Pro（142）键的状态。我们的结果表明，抗体结构域中的内部二硫键通过将折叠核的残基置于邻近位置来限制折叠途径，从而促进了向天然状态的转化。 （c）2006 Elsevier Ltd.保留所有权利。

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