Unrelated de novo enzyme replaces essential enzyme in cell
Iron-rich medium supports the growth of E. coli engineered to no longer have a natural Fes enzyme. They form small, unhealthy, red colonies because they accumulate iron bound to [...]
Iron-rich medium supports the growth of E. coli engineered to no longer have a natural Fes enzyme. They form small, unhealthy, red colonies because they accumulate iron bound to [...]
Electric fields drive the rotating nano-crane – 100,000 times faster than previous methods. (Image: Enzo Kopperger / TUM) Rotation of the arm between two docking points (red [...]
Sixteen topologies of de novo designed hyperstable constrained peptides. Credit: Baker lab, University of Washington Protein design has been one of the major paths from current fabrication technology toward [...]
A review from the group leading recent rapid progress in de novo protein design describes the successes, identifies the remaining challenges, and heralds the advance "from the Stone Age to the Iron Age" in protein design.
Ten designs spanning three types of icosahedral architectures produce atomically precise multi-megadalton protein cages to deliver biological cargo or serve as scaffolds for organizing various molecular functions.
Computational recombination of small elements of structure from known protein structures generates a vast library of designs that balance protein stability with the potential for new functions and novel interactions.
Computer designed networks of hydrogen bonds allow programming specific interactions of protein interfaces, facilitating programming molecular recognition.
A trimeric protein was designed to self assemble into a 60 unit icosahedron with a roomy interior that might find use to ferry molecular cargo into cells or as a chemical reactor.
Recent research documents a structure-based rational design strategy combining molecular dynamics and single molecule imaging to improve the performance of a DNA tweezers that accurately positions an enzyme and its cofactor.
Chains of monomers joined by non-biological peptoid bonds follow different rules of self-assembly and form structures not found in chains joined by the peptide bonds used to form proteins.