Single-molecule visualization determines conformational substate ensembles in β-sheet-rich peptide fibrils

An understanding of protein conformational ensembles is essential for revealing the underlying mechanisms of interpeptide recognition and association. However, experimentally resolving multiple simultaneously existing conformational substates remains challenging. Here, we report the use of scanning...

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Veröffentlicht in:Science advances 2023-07, Vol.9 (27), p.eadg7943-eadg7943
Hauptverfasser: Zhang, Wenbo, Wang, Ruonan, Liu, Mingwei, Li, Shucong, Vokoun, Asher E, Deng, Weichen, Dupont, Robert L, Zhang, Feiyi, Li, Shuyuan, Wang, Yang, Liu, Zhenyu, Zheng, Yongfang, Liu, Shuli, Yang, Yanlian, Wang, Chen, Yu, Lanlan, Yao, Yuxing, Wang, Xiaoguang, Wang, Chenxuan
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Sprache:eng
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Zusammenfassung:An understanding of protein conformational ensembles is essential for revealing the underlying mechanisms of interpeptide recognition and association. However, experimentally resolving multiple simultaneously existing conformational substates remains challenging. Here, we report the use of scanning tunneling microscopy (STM) to analyze the conformational substate ensembles of β sheet peptides with a submolecular resolution (in-plane
ISSN:2375-2548
2375-2548
DOI:10.1126/sciadv.adg7943