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首页> 外文期刊>Journal of Molecular Biology >Does the Location of a Mutation Determine the Ability to Form Amyloid Fibrils?
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Does the Location of a Mutation Determine the Ability to Form Amyloid Fibrils?

机译：突变的位置是否决定形成淀粉样蛋白原纤维的能力？

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摘要

We have previously reported studies of fibril formation by a set of protein G B1 domain (beta1) variants, with mutations located around the central parallel beta-strands. In this study, we designed multiple mutations in the edge strands of beta1 to create proteins with a stability range comparable to that of the set of central mutants. All the edge variants are able to form amyloid fibrils when they are incubated at their melting temperatures. This result suggests that overall protein stability is the key determinant for amyloid formation and not the specific location of destabilizing mutations. The edge strand and variants cross-seed with each other and with members of the central variant family. Interesting fibrillar morphology was observed in some cross-seeding cases and its implications for a better understanding of nucleation and elongation events are discussed.
机译：我们以前曾报道过由一组蛋白质G B1域（beta1）变体形成原纤维的研究，突变位于中央平行β链周围。在这项研究中，我们设计了beta1边缘链中的多个突变，以创建具有与中央突变体组相当的稳定性范围的蛋白质。当所有边缘变体在其解链温度下孵育时，它们都能形成淀粉样原纤维。该结果表明，总体蛋白质稳定性是淀粉样蛋白形成的关键决定因素，而不是破坏稳定突变的特定位置。边缘链和变体彼此杂交，并且与中央变体家族的成员杂交。在一些交叉播种的情况下观察到了有趣的原纤维形态，并讨论了其对更好地理解成核和伸长事件的意义。

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