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Article

The Physical Driving Forces of Conformational Transition for TTR91-96 with Proline Mutations.

Journal of chemical information and modeling - 25 Nov 2024

Cao Yuanming, Xia Pengxuan, Zhu Yanyan, Zhao Qingjie, Li Huiyu

Abstract excerpt

Pathological aggregation of essentially dissociated Transthyretin (TTR) monomer proteins, driven by misfolding and self-interaction, is associated with Transthyretin amyloidosis (ATTR) disease. The TTR monomer proteins consist of several fragments that tend to self-aggregate. Recent experimental studies showed that the sequence of residues TTR91-96 plays an important role in self-aggregation. However, the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 39513968
DOI: 10.1021/acs.jcim.4c01464

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