The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6.

ABSTRACT: Studying folding and assembly of naturally occurring α-helical transmembrane proteins can inspire the design of membrane proteins with defined functions. Thus far, most studies have focused on the role of membrane-integrated protein regions. However, to fully understand folding pathways and stabilization of α-helical membrane proteins, it is vital to also include the role of soluble loops. We have analyzed the impact of interhelical loops on folding, assembly and stability of the heme-containing four-helix bundle transmembrane protein cytochrome b6 that is involved in charge transfer across biomembranes. Cytochrome b6 consists of two transmembrane helical hairpins that sandwich two heme molecules. Our analyses strongly suggest that the loop connecting the helical hairpins is not crucial fo

SUBMITTER: Tome-Stangl L 

PROVIDER: S-EPMC5730185 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature