In protein structures, a beta barrel is a beta sheet composed of tandem repeats that twists and coils to form a closed toroidal structure in which the first strand is bonded to the last strand (hydrogen bond). Beta-strands in many beta-barrels are arranged in an antiparallel fashion. Despite their key biological roles, only a few proteins that fold into lipid membranes have been designed de novo. A class of membrane proteins—transmembrane β barrels (TMBs)—forms a continuous sheet that closes on itself in lipid membranes. In addition to the challenge of designing β-sheet proteins, which are prone to misfolding and aggregation if folding is not properly controlled, the computational design of TMBs is complicated by limited understanding of TMB folding. As a result, no TMB has been designed de novo to date. Using computational methods that incorporate the above insights, scientists have designed TMB sequences that successfully fold and assemble into both detergent micelles and lipid bilayers. Here you can see the crystal structure of a computer designed beta-barrel transmembrane protein (PDB code: 6X9Z).

#molecularart ... #beta ... #barrel ... #membrane ... #design ... #computer ... #xray

Structure rendered with @proteinimaging, post-processed by @stylar.ai_official and depicted with @corelphotopaint