低复杂性蛋白质在均和相隔冷溶液中的构造
C Blake Wilson1, Myungwoon Lee1,2, Wai-Ming Yau1
1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
bioRxiv : the preprint server for biology
|October 7, 2024
概括
在FUS蛋白溶液中,液-液相分离 (LLPS) 不会显著改变局部蛋白质构造. 固态核磁共振在均质和相隔状态中都显示了类似的结构,这表明在LLPS期间的结构稳定性.
科学领域:
- 生物物理学的生物物理.
- 蛋白质科学 蛋白质科学
- 分子生物学分子生物学
背景情况:
- 液-液相分离 (LLPS) 在生物过程和蛋白质生物物理学中至关重要.
- 内在无序的蛋白质,如FUS-LC,经历LLPS,这引发了关于密集阶段的结构变化的问题.
- 高度和相隔滴中的相互作用可能会改变蛋白质构造.
研究的目的:
- 调查FUS-LC.的同质状态和相隔状态之间的局部构造分布是否不同.
- 为了确定LLPS伴随着内在无序蛋白质的构造变化的程度.
- 评估LLPS对当地的蛋白质结构的影响.
主要方法:
- 固态核磁共振 (ssNMR) 光谱学被用来分析FUS-LC.
- 在平衡在LLPS过渡温度以上和以下后,溶液被快速结.
- 动态核极化 (DNP) 增强的ssNMR测量是在低温度 (25 K) 进行的.
主要成果:
- 二维ssNMR光谱显示了对均质和相隔FUS-LC状态的几乎相同的交叉峰值模式.
- 标签策略 (统一,残留物特定,碎片结合) 产生了一致的结果.
- 模拟表明,形状分布的变化是最小的 (≤5-10%).
结论:
- FUS-LC的LLPS不会诱导局部形状分布的实质性变化.
- 固有无序蛋白质的结构完整性在不同的相位状态中保持.
- ssNMR是一种强大的工具,用于探测复杂的生物凝聚物的蛋白质构成.
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