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Aromatic–aromatic interactions drive fold switch of GA95 and GB95 with three residue difference

机译:芳烃-芳烃相互作用驱动 GA95 和 GB95 的折叠转换具有三个残基差异

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摘要

Proteins typically adopt a single fold to carry out their function, but metamorphic proteins, with multiple folding states, defy this norm. Deciphering the mechanism of conformational interconversion of metamorphic proteins is challenging. Herein, we employed nuclear magnetic resonance (NMR), circular dichroism (CD), and all-atom molecular dynamics (MD) simulations to elucidate the mechanism of fold switching in proteins GA95 and GB95, which share 95% sequence homology. The results reveal that long-range interactions, especially aromatic π–π interactions involving residues F52, Y45, F30, and Y29, are critical for the protein switching from a 3α to a 4β + α fold. This study contributes to understanding how proteins with highly similar sequences fold into distinct conformations and may provide valuable insights into the protein folding code.
机译:蛋白质通常采用单个折叠来执行其功能,但具有多个折叠状态的蛋白质违背了这一规范。破译蛋白的构象相互转化的机制具有挑战性。在此,我们采用核磁共振 (NMR) 、圆二色谱 (CD) 和全原子分子动力学 (MD) 模拟来阐明具有 95% 序列同源性的蛋白质 GA95 和 GB95 的折叠切换机制。结果表明,长程相互作用,尤其是涉及残基 F52、Y45、F30 和 Y29 的芳香族 π-π 相互作用,对于蛋白质从 3α 转换为 4β + α 倍至关重要。本研究有助于了解具有高度相似序列的蛋白质如何折叠成不同的构象,并可能为蛋白质折叠密码提供有价值的见解。

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