There is a strand-based evolutionary mechanism for the diversification of outer membrane proteins, which has implications for how repeat proteins are created and for how outer membrane proteins fold.

The range of barrel-shaped proteins found in the outer membrane of certain bacteria evolved through multiple pathways.

Outer membrane β-barrel proteins in Gram-negative bacteria are assembled within the lumen of the BamA β-barrel.

Bacterial outer membrane proteins are recognized by BamD at specific signals located in multiple β-strands at the C-terminus of these proteins, and this recognition is important for efficient outer membrane protein assembly and maintaining the integrity of outer membrane.

A complex that catalyzes the membrane integration of β barrel proteins and a molecular chaperone promote the complete assembly of a bacterial virulence factor in vitro.

Electron and atomic force microscopy show how bacterial toxins bind to a host membrane and assemble into arcs and rings, before undergoing a dramatic, concerted conformational change to insert into the membrane.

The pilus extrusion/DNA uptake system of Thermus thermophilus contains a 13-mer of the 757-residue PilQ protein and a tightly bound protein outside the outer membrane with a role in DNA binding.

A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.

Protein heptosyltransferases modify a group of bacterial autotransporters for virulence function and employ a novel structural mechanism for the processive hyperglycosylation of the autotransporter.

A chemically unstable ostrich eggshell peptide survives for at least 3.8 million years at the equator, stabilized by strong mineral interactions.