本頁只刊出中文翻譯與中文說明；英文原文請見下方原文連結。
原文連結
論文資訊
- 類型：已發表論文
- 日期：2022-10-13
摘要
Chaperones facilitate the folding of other (“client”) 蛋白質s and can thus affect the adaptive 演化 of these clients. Specifically, chaperones affect the phenotype of 蛋白質s via two opposing mechanisms. On the one hand, they can buffer the effects of 突變s in 蛋白質s and thus help preserve an ancestral, pre突變 phenotype. On the other hand, they can potentiate the effects of 突變s and thus enhance the phenotypic changes caused by a 突變. We study that how the 細菌l Hsp90 chaperone (HtpG) affects the 演化 of green fluorescent 蛋白質. To this end, we performed directed 演化 of green fluorescent 蛋白質 under low and high cellular concentrations of Hsp90. Specifically, we evolved green fluorescent 蛋白質 under both stabilizing selection for its ancestral (green) phenotype and directional selection toward a new (cyan) phenotyp
※ 此為已發表論文，全文需透過期刊付費取得