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.
|Original language||English (US)|
|Title of host publication||Methods in Enzymology|
|Publisher||Academic Press Inc.|
|Number of pages||36|
|State||Published - Jan 2021|
|Name||Methods in Enzymology|
Bibliographical noteFunding Information:
We acknowledge funding from the NIH (R35-GM126940 and R01-GM117923 to S.S.)
© 2021 Elsevier Inc.
- ER/K linker
- FRET biosensors
- Protein-protein interactions
- Single alpha helix