Electrostatic and hydrophobic interaction cooperative nanochaperone regulates protein folding

Electrostatic and hydrophobic interaction cooperative nanochaperone regulates protein folding

Abstract Natural molecular chaperones utilize spatially ordered multiple molecular forces to effectively regulate protein folding. However, synthesis of such molecules is a big challenge. The concept of “aggregate science” provides insights to construct chemical entities (aggregates) beyond molecula...

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Bibliographic Details
Main Authors: Xiaohui Wu, Fei Deng, Yujie Chen, Mengchen Xu, Feihe Ma, Linqi Shi
Format: Article
Language:English
Published: Wiley 2024-02-01
Series:Aggregate
Subjects:
chaperone‐like activity
cooperative effect
nanochaperones
ordered aggregates
protein folding
Online Access:https://doi.org/10.1002/agt2.429

Internet

https://doi.org/10.1002/agt2.429

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