Large ears enhance perception of echolocation and prey generated sounds in bats. However, external ears likely impair aerodynamic performance of bats compared to birds. But large ears may generate lift on their own, mitigating the negative effects. We studied flying brown long-eared bats, using high resolution, time resolved particle image velocimetry, to determine the aerodynamics of flying with large ears. We show that the ears and body generate lift at medium to cruising speeds (3-5 m/s), but at the cost of an interaction with the wing root vortices, likely reducing inner wing performance. We also propose that the bats use a novel wing pitch mechanism at the end of the upstroke generating thrust at low speeds, which should provide effective pitch and yaw control. In addition, the wing tip vortices show a distinct spiraling pattern. The tip vortex of the previous wingbeat remains into the next wingbeat and rotates together with a newly formed tip vortex. Several smaller vortices, related to changes in circulation around the wing also spiral the tip vortex. Our results thus show a new level of complexity in bat wakes and suggest large eared bats are less aerodynamically limited than previous wake studies have suggested.
Microscale soft-robots hold great promise as safe handlers of delicate micro-objects but their wider adoption requires micro-actuators with greater efficiency and ease-of-fabrication. Here we present an elastomeric microtube-based pneumatic actuator that can be extended into a microrobotic tentacle. We establish a new, direct peeling-based technique for building long and thin, highly deformable microtubes and a semi-analytical model for their shape-engineering. Using them in combination, we amplify the microtube’s pneumatically-driven bending into multi-turn inward spiraling. The resulting micro-tentacle exhibit spiraling with the final radius as small as ~185 μm and grabbing force of ~0.78 mN, rendering itself ideal for non-damaging manipulation of soft, fragile micro-objects. This spiraling tentacle-based grabbing modality, the direct peeling-enabled elastomeric microtube fabrication technique, and the concept of microtube shape-engineering are all unprecedented and will enrich the field of soft-robotics.
The activity of CTP:phosphocholine cytidylyltransferase (CCT), a key enzyme in phosphatidylcholine synthesis, is regulated by reversible interactions of a lipid-inducible amphipathic helix (domain M) with membrane phospholipids. When dissociated from membranes a portion of the M domain functions as an auto-inhibitory (AI) element to suppress catalysis. The AI helix from each subunit binds to a pair of α-helices (αE) that extend from the base of the catalytic dimer to create a four-helix bundle. The bound AI helices make intimate contact with loop L2, housing a key catalytic residue, Lys-122. The impacts of the AI helix on active-site dynamics and positioning of Lys-122 are unknown. Extensive MD simulations with and without the AI helix revealed that backbone carbonyl oxygens at the point of contact between the AI helix and loop L2 can entrap the Lys-122 side chain, effectively competing with the substrate, CTP. In silico, removal of the AI helices dramatically increased αE helix dynamics at a predicted break in the middle of these helices, enabling them to splay apart and forge new contacts with loop L2. In vitro cross-linking confirmed the reorganization of the αE element upon membrane binding of the AI helix. Moreover, when αE bending was prevented by disulfide engineering, CCT activation by membrane binding was thwarted. These findings suggest a novel two-part auto-inhibitory mechanism for CCT involving capture of Lys-122 and restraint of the pliable αE helices. We propose that membrane binding enables bending of the αE helices, bringing the active site closer to the membrane surface.
Mirrored carbon-spirals have been produced from pressured ferrocene via the bilateral extrusion of the spiral pairs from an iron core. A parametric plot of the surface geometry displays the fractal growth of the conical helix made with the logarithmic spiral. Electron microscopy studies show the core is a crystalline cementite which grows and transforms its shape from spherical to biconical as it extrudes two spiralling carbon arms. In a cross section along the arms we observe graphitic flakes arranged in a herringbone structure, normal to which defects propagate. Local-wave-pattern analysis reveals nanoscale defect patterns of two-fold symmetry around the core. The data suggest that the bilateral growth originates from a globular cementite crystal with molten surfaces and the nano-defects shape emerging hexagonal carbon into a fractal structure. Understanding and knowledge obtained provide a basis for the controlled production of advanced carbon materials with designed geometries.
Piezo1 and Piezo2 are mechanically activated ion channels that mediate touch perception, proprioception and vascular development. Piezos are distinct from other ion channels and their structure remains poorly defined, impeding detailed study of their gating and ion permeation properties. Here we report a high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer. The detergent-solubilized complex adopts a three-blade propeller shape with a curved transmembrane region containing at least 26 transmembrane helices per protomer. The flexible propeller blades can adopt distinct conformations, and consist of a series of four-transmembrane helix bundles we term ‘Piezo repeats’. Carboxy-terminal domains line the central ion pore, and the channel is closed by constrictions in the cytosol. A kinked helical beam and anchor domain link the Piezo repeats to the pore, and are poised to control gating allosterically. The structure provides a springboard to dissect further how Piezos are regulated by mechanical force.
Two-dimensional (2D) materials can uniquely span the physical dimensions of a surrounding composite matrix in the limit of maximum reinforcement. However, the alignment and assembly of continuous 2D components at high volume fraction remain challenging. We use a stacking and folding method to generate aligned graphene/polycarbonate composites with as many as 320 parallel layers spanning 0.032 to 0.11 millimeters in thickness that significantly increases the effective elastic modulus and strength at exceptionally low volume fractions of only 0.082%. An analogous transverse shear scrolling method generates Archimedean spiral fibers that demonstrate exotic, telescoping elongation at break of 110%, or 30 times greater than Kevlar. Both composites retain anisotropic electrical conduction along the graphene planar axis and transparency. These composites promise substantial mechanical reinforcement, electrical, and optical properties at highly reduced volume fraction.
Disulfide bridge formation was investigated in helical aromatic oligoamide foldamers. Depending on the position of thiol-bearing side chains, exclusive intramolecular or intermolecular disulfide bridging may occur. The two processes are capable of self-sorting, presumably by dynamic exchange. Quantitative assessment of helix handedness inversion rates showed that bridging stabilizes the folded structures. Intermolecular disulfide bridging serendipitously yielded a well-defined, C2 -symmetrical, two-helix bundle-like macrocyclic structure in which complete control over relative handedness, that is, helix-helix handedness communication, is mediated remotely by the disulfide bridged side chains in the absence of contacts between helices. MM calculations suggest that this phenomenon is specific to a given side chain length and requires disulfide functions.
Plant-based bio-inspired magnetically-propelled helical microswimmers are described. The helical microstructures are derived from spiral water-conducting vessels of different plants, harnessing the intrinsic biological structures of Nature. Geometric variables of the spiral vessels, such as the helix diameter and pitch, can be controlled by mechanical stretching for the precise fabrication and consistent performance of helical microswimmers. Xylem vessels of a wide variety of different plants have been evaluated for the consistency and reproducibility of their helical parameters. Sequential deposition of thin Ti and Ni layers directly on the spiral vessels, followed by dicing, leads to an extremely simple and cost-efficient mass-production of functional helical microswimmers. The resulting plant-based magnetic microswimmers display efficient propulsion, with a speed of over 250 µm/s, as well as powerful locomotion in biological media such as human serum. The influence of actuation frequencies on the swimming velocity is investigated. Such use of plant vessels results in signiﬁcant savings in the processing costs and provides an extremely simple, cost-effective fabrication route for the large-scale production of helical magnetic swimmers.
In eukaryotes, the Cdt1-bound replicative helicase core MCM2-7 is loaded onto DNA by the ORC-Cdc6 ATPase to form a prereplicative complex (pre-RC) with an MCM2-7 double hexamer encircling DNA. Using purified components in the presence of ATP-γS, we have captured in vitro an intermediate in pre-RC assembly that contains a complex between the ORC-Cdc6 and Cdt1-MCM2-7 heteroheptamers called the OCCM. Cryo-EM studies of this 14-subunit complex reveal that the two separate heptameric complexes are engaged extensively, with the ORC-Cdc6 N-terminal AAA+ domains latching onto the C-terminal AAA+ motor domains of the MCM2-7 hexamer. The conformation of ORC-Cdc6 undergoes a concerted change into a right-handed spiral with helical symmetry that is identical to that of the DNA double helix. The resulting ORC-Cdc6 helicase loader shows a notable structural similarity to the replication factor C clamp loader, suggesting a conserved mechanism of action.
The mechanosensitive Piezo channels function as key eukaryotic mechanotransducers. However, their structures and mechanogating mechanisms remain unknown. Here we determine the three-bladed, propeller-like electron cryo-microscopy structure of mouse Piezo1 and functionally reveal its mechanotransduction components. Despite the lack of sequence repetition, we identify nine repetitive units consisting of four transmembrane helices each-which we term transmembrane helical units (THUs)-which assemble into a highly curved blade-like structure. The last transmembrane helix encloses a hydrophobic pore, followed by three intracellular fenestration sites and side portals that contain pore-property-determining residues. The central region forms a 90 Å-long intracellular beam-like structure, which undergoes a lever-like motion to connect THUs to the pore via the interfaces of the C-terminal domain, the anchor-resembling domain and the outer helix. Deleting extracellular loops in the distal THUs or mutating single residues in the beam impairs the mechanical activation of Piezo1. Overall, Piezo1 possesses a unique 38-transmembrane-helix topology and designated mechanotransduction components, which enable a lever-like mechanogating mechanism.