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.
Archive for the 'Bionanotechnology' Category
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.
An engineered protein controls the assembly of C60 fullerene molecules into an atomically precise lattice that conducts electricity while neither component alone would.
Computational design of an enzyme that carboligates three one-carbon molecules to form one three-carbon molecule, an activity that does not exist in nature, provides proof-of-principle for a novel metabolic pathway for carbon fixation.
A DNA strand capable of forming a triple helix with a portion of the DNA double helices in a macroscopic DNA crystal enhances the weak interactions holding the crystal together so that the crystal remains stable in the absence of a high ionic strength environment.
A specially designed triplex forming oligonucleotide bearing a cargo molecule binds to a specific sequence in the major groove of a DNA double helix to form a modified DNA tile that self assembles into a macroscopic crystal in which each helix carries a cargo molecule positioned to sub-nanometer precision.
Structural DNA nanotechnology: progress toward a precise self-assembling three dimensional scaffold by building macroscopic crystals from nanoscale structures.
Small, stiff, rectangular rods made using scaffolded DNA origami bypass drug resistance mechanisms in the membranes of a cultured leukemia cell line and release enough therapeutic drug to kill the cancer cell.
California Institute of Technology is holding a symposium to honor Paul Rothemund’s seminal contribution to the field of DNA nanotechnology: the research paths opened by the technology, and where they might lead.
Thousands of amateurs playing the online RNA folding game Eterna, backed up by a real-world automated lab testing their predictions, have provided insights to improve the algorithms computers use to design RNA molecules.
A rotor with DNA origami parts held together by an engineered tight fit instead of by covalent bonds can revolve freely, driven by Brownian motion and dwelling at engineered docking sites.
Two research teams present two different methods for using single strands of DNA to link various nanoparticles into complex 3D arrays: one using DNA hairpins for dynamic reconfiguration and the other using a DNA origami scaffold.
Encapsulating enzymes in nanocages engineered using structural DNA nanotechnology increases enzymatic digestion and protects enzymes from degradation.
Polymer chemistry and materials research provide opportunities to explore structures that harmonize phenomena unique to nanoscale technology, the role of mechanical forces generated at interfaces, and the responses of biological systems to mechanical stresses.
New families of protein structures, barrel proteins for positioning small molecules, self-assembling protein arrays, and precision sculpting of protein architectures highlight de novo protein design advances.
Computational design of proteins satisfying predetermined geometric constraints produced stable proteins with the designed structure that are not found in nature.
A fully automated design protocol generates dozens of designs for proteins based on helix-loop-helix-loop repeat units that are very stable, have crystal structures that match the design, have very different overall shapes, and are unrelated to any natural protein.