Engineering a Novel Porin OmpGF Via Strand Replacement from Computational Analysis of Sequence Motif.

ABSTRACT: β-Barrelmembrane proteins (βMPs) form barrel-shaped pores in the outer membrane of Gram-negative bacteria, mitochondria, and chloroplasts. Because of the robustness of their barrel structures, βMPs have great potential as nanosensors for single-molecule detection. However, natural βMPs currently employed have inflexible biophysical properties and are limited in their pore geometry, hindering their applications in sensing molecules of different sizes and properties. Computational engineering has the promise to generate βMPs with desired properties. Here we report a method for engineering novel βMPs based on the discovery of sequence motifs that predominantly interact with the cell membrane and appear in more than 75% of transmembrane strands. By replacing β1-β6 strands of the protein OmpF t

SUBMITTER: Lin M 

PROVIDER: S-EPMC5434230 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature