Unrelated de novo enzyme replaces essential enzyme in cell

The first proposal of a path from then current technology to the ability to fabricate complex materials and devices by placing the atoms where you want them was made by Richard Feynman in 1959: “There’s Plenty of Room at the Bottom“, but see also this series “Feynman Path to Nanotechnology“. The second proposal to achieve… Continue reading Unrelated de novo enzyme replaces essential enzyme in cell

Ultrafast DNA robotic arm: A step toward a nanofactory?

Ultrafast molecular machines made using DNA nanotechnology have now been demonstrated. Over the past several years molecular machines made using DNA nanotechnology, especially the scaffolded DNA origami technology, have grown more complex and more functional (see, for example, here, here, here, and here). Long-time Foresight member Dr. Robert P. Meagley writes to point out that… Continue reading Ultrafast DNA robotic arm: A step toward a nanofactory?

Design of hyperstable constrained peptides

Protein design has been one of the major paths from current fabrication technology toward the goal of general purpose, high-throughput atomically precise manufacturing since Foresight co-founder Eric Drexler proposed it in 1981. It also produced some of the earliest promising results. Although de novo protein design was at first slow, progress has accelerated since David… Continue reading Design of hyperstable constrained peptides

From de novo protein design to molecular machine systems

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.

Two-component, 120-subunit icosahedral cage extends protein nanotechnology

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.

Designing novel protein backbones through digital evolution

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.

Adding modular hydrogen-bond networks to protein design

Computer designed networks of hydrogen bonds allow programming specific interactions of protein interfaces, facilitating programming molecular recognition.

Assembling a large, stable, icosahedral protein molecular cage

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.

Rational improvement of DNA nanodevice function

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.

Peptoid nanosheets assemble by different design rule

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.

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