category
Nature Communications
date
Mar 2, 2026
slug
status
Published
summary
首次通过氢/氘交换质谱与溶液核磁共振联用技术,揭示了Bpa的组装动态及其与底物的相互作用机制,填补了该蛋白结构异质性研究的空白。
tags
蛋白质组学
type
Post

📄 原文题目

Structural heterogeneity and substrate engagement mechanism of the bacterial proteasome activator Bpa

🔗 原文链接

💡 AI 核心解读

首次通过氢/氘交换质谱与溶液核磁共振联用技术,揭示了Bpa的组装动态及其与底物的相互作用机制,填补了该蛋白结构异质性研究的空白。

📝 英文原版摘要

<p>Nature Communications, Published online: 02 March 2026; <a href="https://www.nature.com/articles/s41467-026-69978-w">doi:10.1038/s41467-026-69978-w</a></p>Bpa (bacterial proteasome activator) is essential for Mycobacterium tuberculosis virulence, yet its structural heterogeneity and mode of substrate engagement have remained poorly understood. Here, the authors combine hydrogen/deuterium exchange mass spectrometry and solution NMR spectroscopy to elucidate Bpa assembly and its interaction with a model substrate.
破解O-GlcNA糖基化网络的密码实验与模拟FRAP用于螺旋细胞中蛋白质扩散的定量测定
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