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Decoupling sequence and structure
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DOI：10.1038/s41570-025-00726-2.png)
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Abstract
En 中文
In 1961, it was demonstrated that the enzyme ribonuclease can correctly fold upon oxidation in air from a fully reduced and denatured polypeptide chain. Since then, the principles that govern the oxidative folding of polypeptide chains have been elucidated, and our ability to control this process has advanced significantly.
Journal
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51.7
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1.0K
Citations:
1.9W
Organization
Cited Papers
Motif-Directed Oxidative Folding to Design and Discover Multicyclic Peptides for Protein Recognition
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ShareSaveReagentless Oxidative Folding of Disulfide-Rich Peptides Catalyzed by an Intramolecular Diselenide
OAAI
OAAIShareSaveTwin disulfides for orthogonal disulfide pairing and the directed folding of multicyclic peptides.png)
NATURE CHEMISTRY
NATURE CHEMISTRYIF20.2
PREAI
ShareSaveTHE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAINOAAI
OAAIShareSaveShareSaveMammalian display screening of diverse cystine-dense peptides for difficult to drug targetsNATURE COMMUNICATIONSOAAI
NATURE COMMUNICATIONSIF15.7
OAAIShareSaveDisulfide-Directed Multicyclic Peptide Libraries for the Discovery of Peptide Ligands and Drugs
PREAI
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