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May 15, 2026Analytical Chemistry0 citations

Chemical Redirection of Protein Folding Landscapes via Lysine-Targeted Induction of Helix-to-Sheet Transitions

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RZRui ZhaoLRLixia RenXSXiangjun Si

Key Points

  • This study aims to explore ways to manipulate protein folding pathways and their aggregation behaviors.
  • Utilized HCCs for probing protein conformational changes
  • Induced helix-to-sheet transitions in lysozyme
  • Analyzed effects on catalytic activity and aggregation
  • Successfully redirected protein folding landscapes via targeted modifications
  • Clarified the relationship between protein topology and proteotoxicity
  • Provided insights into regulatory mechanisms of protein homeostasis

Abstract

catalytic activity and the regulation of amyloidogenic aggregation in lysozyme. Our findings establish HCCs as a versatile platform for interrogating protein conformational landscapes and provide a synthetic strategy to manipulate protein topology. This approach opens new avenues for protein engineering and offers deep insights into the fundamental principles governing protein homeostasis and the molecular basis of proteotoxicity.

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Cite This Study

Zhao et al. (2026) studied this question.

synapsesocial.com/papers/6a06b86ae7dec685947aae61https://doi.org/10.1021/acs.analchem.6c00550
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