Nature Communications · 2019 · 102 citations · 22 references
Life SciencesBioengineeringMolecular BiologyMolecular VirologyStructural BiologySynthetic BiologyMacromolecular AssemblyMacromolecular StructureMolecular CapsulesMolecular MachinesProtein StructureProtein ThreadingArtificial Molecular MachinesCapsule AssemblyCavity EnlargementPeptide FoldingPeptide Self-assemblySphere PackingThreading
Abstract Cavity creation is a key to the origin of biological functions. Small cavities such as enzyme pockets are created simply through liner peptide folding. Nature can create much larger cavities by threading and entangling large peptide rings, as learned from gigantic virus capsids, where not only chemical structures but the topology of threaded rings must be controlled. Although interlocked molecules are a topic of current interest, they have for decades been explored merely as elements of molecular machines, or as a synthetic challenge. No research has specifically targeted them for, and succesfully achieved, cavity creation. Here we report the emergence of a huge capsular framework via multiple threading of metal–peptide rings. Six equivalent C 4 -propeller-shaped rings, each consisting of four oligopeptides and Ag + , are threaded by each other a total of twelve times (crossing number: 24) to assemble into a well-defined 4 nm-sized sphere, which acts as a huge molecular capsule.
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A short history of<i>SHELX</i>
George M. Sheldrick · Acta Crystallographica Section A Foundations of Crystallography · 2007 · 87.4K citations · Full text
Topologically Linked Protein Rings in the Bacteriophage HK97 Capsid
William R. Wikoff, Lars Liljas, Robert L. Duda et al. · Science · 2000 · 733 citations