NanoTubAR vs Crys

"Nanoscience" is the branch of science that is responsible for the study of objects at the nanometric scale, that is, those whose sizes are between 1 and 100 nm. One of the great challenges of nanotechnology is the preparation of new functional materials whose dimensions and structures are controlled at the molecular or atomic level. In chemistry, nanotubes are tubular (cylindrical) structures, with typical diameter sizes in the scale of a nanometer. There are nanotubes of many materials. Among the best-known are carbon nanotubes (CNT) made up of rolled sheets of carbon atoms, with physical and chemical properties that open the door to an immense horizon of applications. In addition to CNTs, there are nanotubes formed by the self-assembly of cyclic peptides. This type of nanostructures has attracted great attention from the scientific community in recent years due to their important applications in biology, chemistry and materials science. Much of this interest is related to its technological possibilities such as biosensors, photosensitive materials, antimicrobial agents, selective transport systems, molecular electronics and other potential uses in biology, electronics and optics. The history of these nanotubes began in 1974, when De Santis predicted the formation of tubular structures by cyclic peptides, formed by alpha amino acids with alternating stereochemistry, D and L (D, L-α-CPs). However, it was not until 1993 when they were prepared in a laboratory thanks to Professor Ghadiri's group at Scripps. Their applications comprehend those that involve interaction with membranes, including the use as antimicrobials or as biomimetics of natural channels. Their hydrophilic internal cavity facilitates the transport of water and hydrophilic molecules of appropriate size, such as ions or drugs. The external properties of the nanotube are defined by the side chains of the amino acids that make up the cyclic peptide, oriented towards the outside. More recently, in the group of Prof. Juan R. Granja, at the University of Santiago de Compostela, nanotubes formed by cyclic peptides that alternate alpha amino acids with other types of artificial amino acids, such as gamma (α, γ-CPs) or delta (α, δ-CPs) have been designed and synthesized. This type of non-natural amino acids allows methylene groups to be introduced into the cavity of the channels, increasing their hydrophobicity and allowing their internal functionalization. NanotubAR allows to visualize, using Augmented Reality technology, four types of nanotubes: a carbon nanotube (CNT) and three nanotubes formed by cyclic peptides. The representation of the nanotubes included in the app are not just cartoons, they come from realistic atomistic models resulting from computational simulations. In each of them, natural alpha amino acids (L-tryptophan) are combined with synthetic residues, such as D-tryptophan (D, L-alpha-CPs), gamma amino acids (alpha, gamma-CPs) and delta amino acids (alpha, delta -CPs). In all these designs, the amino and carbonyl groups of the amino acids are oriented perpendicularly to the plane of the cyclic peptides, with a suitable orientation to establish hydrogen bonds between the different units, and thus forming a tubular structure. With NanotubAR it is possible to obtain a privileged view of these systems in our own home, or anywhere, from a simple texture, walk around it, and even enter its inner cavity to be able to observe its interior structure in detail at a level atomistic detail. In addition, NanotubAR allows changing the representation of the atoms that make up the systems and choosing between “ball and stick” or a van der Waals representation. Delve into nanotechnology and share with your friends a photo inside your favorite nanotube!

Crys-CAST brings crystal and molecular structure viewing, geometry analysis, and presentation tools to iPhone and iPad. OPEN AND EXPLORE Open CIF, XYZ, PDB, MOL, SDF, MOL2, and RES files from Files or other apps. Explore asymmetric units, unit cells, and supercells with ball-and-stick, Spacefill, coordination polyhedra, and thermal ellipsoids when suitable displacement data is available. Rotate, zoom, and view structures along crystallographic directions. MEASURE AND ANALYZE Inspect bond lengths, bond angles, and geometric hydrogen-bond candidates, grouped by type with clear symmetry details. Combine selected length, angle, and hydrogen-bond labels directly on the structure. Distinguish coordinate-calculated values from matching CIF-reported geometry, and export compact bond-length and bond-angle tables as TXT or Excel-compatible CSV. Explore simulated powder X-ray diffraction patterns, BFDH morphology, and geometric pore analysis. Display pore space alone or together with the crystal structure. BUILD YOUR COLLECTION Organize structures in My Database. Add files from History or import structure files and ZIP, RAR, or 7z archives into a chosen collection. Name entries, save viewing states, and export collections for reuse. CREATE PRESENTATION MATERIALS Save structure images and record GIF or MP4 animations with resolution and frame-rate presets and custom duration. Use automatic rotation or adjust the view while recording. Animation exports contain the structure viewer without interface controls or sound. MAKE THE VIEW YOUR OWN Use a consistent interface on iPhone and iPad, choose light or dark appearance, and customize backgrounds, unit-cell lines, axes, and scale bars. SCIENTIFIC SCOPE Calculated geometry, hydrogen-bond candidates, pore results, and other analyses depend on the input data and selected settings. They support visualization and interpretation but do not replace structure refinement or experimental validation. Missing hydrogen positions are not inferred. Actual recording frame rate depends on device performance and structure complexity.