Intrinsically disordered proteins (IDPs) and the impact on cell stress resistance / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1490-1505, 2022.
Article
Dans Chinois
| WPRIM
| ID: wpr-927795
ABSTRACT
Intrinsically disordered proteins (IDPs) are proteins or protein regions that fail to get folded into definite three-dimensional structures but participate in various biological processes and perform specific functions. Defying the traditional protein "sequence-structure-function" paradigm, they enrich the protein "structure-function" diversity. Ubiquitous in organisms, they show extreme hydrophilicity, charged amino acids, and highly repetitive amino acid sequences, with simple arrangement. As a result, they feature highly variable binding affinities and high coordination, which facilitate their functions. IDPs play an important role in cell stress response, which can improve the tolerance to a variety of stresses, such as freezing, high salt, heat shock, and desiccation. In this study, we briefed the characteristics, classifications, and identification of IDPs, summarized the molecular mechanism in improving cell stress resistance, and described the potential applications.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Conformation des protéines
/
Protéines intrinsèquement désordonnées
/
Congélation
Type d'étude:
Étude pronostique
langue:
Chinois
Texte intégral:
Chinese Journal of Biotechnology
Année:
2022
Type:
Article
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