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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Conformational constraints for amyloid fibrillation: the importance of being unfolded
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Conformational constraints for amyloid fibrillation: the importance of being unfolded

机译：淀粉样蛋白原纤化的构象限制：展现的重要性

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摘要

Recent reports give strong support to the idea that amyloid fibril formation and the subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. In this review, recent findings are surveyed to illustrate that protein fibrillogenesis requires a partially folded conformation. This amyloidogenic conformation is relatively unfolded, and shares many structural properties with the pre-molten globule state, a partially folded intermediate frequently observed in the early stages of protein folding and under some equilibrium conditions. The inherent flexibility of such an intermediate is essential in allowing the conformational rearrangements necessary to form the core cross-beta structure of the amyloid fibril.
机译：最近的报道强烈支持淀粉样蛋白原纤维形成和随后的蛋白质沉积疾病发展源自相应淀粉样蛋白生成蛋白构象变化的观点。在这篇综述中，对最近的发现进行了调查，以说明蛋白质原纤维形成需要部分折叠的构象。这种淀粉样蛋白形成的构象是相对展开的，并且与熔融前的小球状态具有许多结构特性，在蛋白质折叠的早期和某些平衡条件下经常观察到部分折叠的中间物。这种中间体的固有挠性对于允许形成淀粉样原纤维的核心交叉β结构所必需的构象重排至关重要。

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