It is technically difficult to identify transport proteins, but here a method is presented that exploits the principle that they are stabilized in detergent solution when they bind their substrate.

HLA-B*35:01 molecules that are peptide-deficient are thermostable, bind CD8 with higher affinity than their peptide-filled versions, accumulate at immunological synapses and enhance antigen-specific CD8+ T cell immune responses.

A simple, yet elegant method for robust self-assembly of diverse membrane proteins into soluble peptide nanoparticles for their structural and functional analysis in detergent-free solutions.

Chemical perturbation-dependent deep mutational scanning data collected by a lab-based interdisciplinary graduate class resolves a paradox between the high evolution conservation and the high mutational tolerance of the protein ubiquitin.

A comparative study of modern proteins identifies 40 fragments that may represent the observable remnants of a primordial RNA-peptide world.

Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.

Parallel horizontal gene transfer has spread a bacteriolytic gene family to all domains of life, and has bestowed a niche-transcending adaptation in recipients that must deploy antibacterial molecules to survive in a bacterial world.

By combining structure-based computational predictions and a thorough structural analysis, a highly thermostable enzyme, alcohol dehydrogenase, has been engineered.

Rodent herpesvirus Peru overcomes NK ‘missing-self’ killing using a non-classical MHC-I like protein resistant todownregulation by its own ubiquitin ligase that potently sabotages antigen presentation to T-cells.

Histone-lysine N-methyltransferase SETD3 (NP_115609.2) was identified as the actin-specific histidine N-methyltransferase, an enzyme catalyzing the extremely well-conserved methylation of H73 in β-actin.