溶剂化
残留物(化学)
过渡(遗传学)
淀粉样蛋白(真菌学)
激发
化学
生物物理学
化学物理
生物化学
生物
物理
无机化学
量子力学
溶剂
基因
作者
Sonal R More,Santosh Kumar Jha
标识
DOI:10.1021/acs.jpcb.4c07067
摘要
Changes in water-protein interactions are crucial for proteins to achieve functional and nonfunctional conformations during structural transitions by modulating local stability. Amyloid-like protein aggregates in deteriorating neurons are hallmarks of neurodegenerative disorders. These aggregates form through significant structural changes, transitioning from functional native conformations to supramolecular cross-β-sheet structures via misfolded and oligomeric intermediates in a multistep process. However, the site-specific dynamics of water molecules from the native to misfolded conformations and further to oligomeric and compact amyloid structures remain poorly understood. In this study, we used the fluorescence method known as red-edge excitation shift (REES) to investigate the solvation dynamics at specific sites in various equilibrium conformations en route to the misfolding and aggregation of the functional domain of the TDP-43 protein (TDP-43
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