The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity.

ABSTRACT: The de novo design of integral membrane proteins remains a major challenge in protein chemistry. Here, we describe the bottom-up design of a genetically-encoded synthetic membrane protein comprising only four amino acids (L, S, G and W) in the transmembrane domains. This artificial sequence, which we call REAMP for recombinantly expressed artificial membrane protein, is a single chain of 133 residues arranged into four antiparallel membrane-spanning α-helices. REAMP was overexpressed in Escherichia coli and localized to the cytoplasmic membrane with the intended transmembrane topology. Recombinant REAMP could be extracted from the cell membrane in detergent micelles and was robust and stable in vitro, containing helical secondary structure consistent with the original design. Engineered mo

SUBMITTER: Lalaurie CJ 

PROVIDER: S-EPMC6167376 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature