Conjugate of Thiol and Guanidyl Units with Oligoethylene Glycol Linkage for Manipulation of Oxidative Protein Folding

Oxidative protein folding is a biological process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues. In a cell, disulfide-catalysts such as protein disulfide isomerase promote the oxidative protein folding. Inspired by the active sites of the dis...

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Autors principals:	Shunsuke Okada, Motonori Matsusaki, Masaki Okumura, Takahiro Muraoka
Format:	Artigo
Idioma:	Inglês
Publicat:	MDPI AG 2021-02-01
Col·lecció:	Molecules
Matèries:	oxidative protein folding disulfide bond thiol group oligoethylene glycol
Accés en línia:	https://www.mdpi.com/1420-3049/26/4/879
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