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Updated: Sep 24, 2025

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Published on: February 3, 2022

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Mutation-induced change in chignolin stability from π-turn to α-turn

Yutaka Maruyama1, Shunpei Koroku2, Misaki Imai3

  • 1Architecture Development Team, FLAGSHIP 2020 Project, RIKEN Center for Computational Science Kobe 650-0047 Japan.

RSC Advances
|May 6, 2022
PubMed
Summary

Mutating the 8th residue of chignolin to neutral amino acids stabilizes the misfolded state. This peptide engineering strategy successfully created stable misfolded structures, demonstrating control over protein folding pathways.

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