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Updated: Sep 12, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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护送功能的核心蛋白质动力学:来自溶液NMR的见解

Piao Ge1, Li Dai1, Charalampos G Kalodimos2

  • 1Ministry of Education Key Laboratory for Membrane-less Organelles & Cellular Dynamics, Center for Advanced Interdisciplinary Science and Biomedicine of IHM, Biomedical Sciences and Health Laboratory of Anhui Province, Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, 230027 Hefei, PR China.

Journal of molecular biology
|August 8, 2025
PubMed
概括

分子陪伴者通过动态相互作用来维持细胞蛋白质稳定. 先进的NMR光谱学揭示了蛋白质动力学如何对伴侣功能,客户端识别和细胞适应性至关重要.

关键词:
陪伴者与客户的互动构造动力学 构造动力学分子的陪伴者是分子的陪伴者.解决方案NMR是NMR的解决方案.

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