连接器
生物物理学
功能(生物学)
化学
分子动力学
蛋白质-蛋白质相互作用
计算生物学
纳米技术
生物
生物化学
细胞生物学
材料科学
计算机科学
计算化学
操作系统
作者
Tejas M. Gupte,Michael Ritt,Sivaraj Sivaramakrishnan
出处
期刊:Methods in Enzymology
日期:2021-01-01
卷期号:: 173-208
被引量:4
标识
DOI:10.1016/bs.mie.2020.10.002
摘要
ER/K α-helices are a subset of single alpha helical domains, which exhibit unusual stability as isolated protein secondary structures. They adopt an elongated structural conformation, while regulating the frequency of interactions between proteins or polypeptides fused to their ends. Here we review recent advances on the structure, stability and function of ER/K α-helices as linkers (ER/K linkers) in native proteins. We describe methodological considerations in the molecular cloning, protein expression and measurement of interaction strengths, using sensors incorporating ER/K linkers. We highlight biological insights obtained over the last decade by leveraging distinct biophysical features of ER/K-linked sensors. We conclude with the outlook for the use of ER/K linkers in the selective modulation of dynamic cellular interactions.
科研通智能强力驱动
Strongly Powered by AbleSci AI