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首页> 外文期刊>Journal of Molecular Biology >Two immunoglobulin tandem proteins with a linking β-strand reveal unexpected differences in cooperativity and folding pathways
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Two immunoglobulin tandem proteins with a linking β-strand reveal unexpected differences in cooperativity and folding pathways

机译：具有连接的β链的两种免疫球蛋白串联蛋白揭示了协同作用和折叠途径中的意外差异

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摘要

The study of the folding of single domains, in the context of their multidomain environment, is important because more than 70% of eukaryotic proteins are composed of multiple domains. The structures of the tandem immunoglobulin (Ig) domain pairs A164-A165 and A168-A169, from the A-band of the giant muscle protein titin, reveal that they form tightly associated domain arrangements, connected by a continuous β-strand. We investigate the thermodynamic and kinetic properties of these tandem domain pairs. While A164-A165 apparently behaves as a single cooperative unit at equilibrium, unfolding without the accumulation of a large population of intermediates, domains in A168-A169 behave independently. Although A169 appears to be stabilized in the tandem protein, we show that this is due to nonspecific stabilization by extension. We elucidate the folding and unfolding pathways of both tandem pairs and show that cooperativity in A164-A165 is a manifestation of the relative refolding and unfolding rate constants of each individual domain. We infer that the differences between the two tandem pairs result from a different pattern of interactions at the domain/domain interface.
机译：在多域环境中研究单域折叠非常重要，因为超过70％的真核蛋白由多个域组成。串联免疫球蛋白（Ig）结构域对A164-A165和A168-A169的结构来自巨型肌肉蛋白titin的A带，显示它们形成紧密相关的结构域排列，由连续的β链连接。我们研究了这些串联域对的热力学和动力学性质。尽管A164-A165在平衡时表现为单个协作单元，但在不积累大量中间体的情况下展开，而A168-A169中的结构域则独立发挥作用。虽然A169在串联蛋白中似乎稳定，但我们证明这是由于延伸引起的非特异性稳定。我们阐明了两个串联对的折叠和展开路径，并表明A164-A165中的协同作用是每个单个结构域的相对重折叠和展开速率常数的体现。我们推断两个串联对之间的差异是由于域/域接口处的交互方式不同而导致的。

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