Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway
펼치기 Authors and Affiliations

To understand membrane protein biogenesis, we need to explore folding within a bilayer context. Here, we describe a single-molecule force microscopy technique that monitors the folding of helical membrane proteins in vesicle and bicelle environments. After completely unfolding the protein at high force, we lower the force to initiate folding while transmembrane helices are aligned in a zigzag manner within the bilayer, thereby imposing minimal constraints on folding. We used the approach to characterize the folding pathways of the Escherichia coli rhomboid protease GlpG and the human β2-adrenergic receptor. Despite their evolutionary distance, both proteins fold in a strict N-to-C-terminal fashion, accruing structures in units of helical hairpins. These common features suggest that integral helical membrane proteins have evolved to maximize their fitness with cotranslational folding.

논문정보   F1000선정
- 형식: Research article
- 게재일: 2019년 11월 (BRIC 등록일 2019-11-29)
- 연구진: 국내(교신)+국외 연구진태극기
댓글 (0)
웨비나 참석자 모집중...
HOME   |   이용약관   |   개인정보처리방침