When a spilled drop of coffee dries on a solid surface, it leaves a dense, ring-like deposit along the perimeter (Fig 1a) The coffee—initially dispersed over the entire drop—becomes concentrated into a tiny fraction of it Such ring deposits are common wherever drops containing dispersed solids evaporate on a surface, and they influence processes such as printing, washing and coating1,2,3,4,5 Ring deposits also provide a potential means to write or deposit a fine pattern onto a surface Here we ascribe the characteristic pattern of the deposition to a form of capillary flow in which pinning of the contact line of the drying drop ensures that liquid evaporating from the edge is replenished by liquid from the interior The resulting outward flow can carry virtually all the dispersed material to the edge This mechanism predicts a distinctive power-law growth of the ring mass with time—a law independent of the particular substrate, carrier fluid or deposited solids We have verified this law by microscopic observations of colloidal fluids

/pdf/capillary-flow-as-the-cause-of-ring-stains-from-dried-liquid-5dw0ckou95.pdf

Capillary flow as the cause of ring stains from dried liquid drops

Core/Shell Nanoparticles: Classes, Properties, Synthesis Mechanisms, Characterization, and Applications

Recent advances in the exploitation of localized surface plasmons (charge density oscillations confined to metallic nanoparticles and nanostructures) in nanoscale optics and photonics, as well as in the construction of sensors and biosensors, are reviewed here. In particular, subsequent to brief surveys of the most-commonly used methods of preparation and arraying of materials with localized surface plasmon resonance (LSPR), and of the optical manifestations of LSPR, attention will be focused on the exploitation of metallic nanostructures as waveguides; as optical transmission, information storage, and nanophotonic devices; as switches; as resonant light scatterers (employed in the different near-field scanning optical microscopies); and finally as sensors and biosensors.

Exploitation of Localized Surface Plasmon Resonance

An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic β subunits that support the binding change mechanism with an internal rotation of the γ subunit. Other structural and mutational probes of the F1 and F0 portions of the ATP synthase are reviewed, together with kinetic and other evaluations of catalytic site occupancy and behavior during hydrolysis or synthesis of ATP. Subunit function as related to proton translocation and rotational catalysis is considered. Physical demonstrations of the γ subunit rotation have been achieved. The findings have implications for other enzymatic catalyses.

/pdf/the-atp-synthase-a-splendid-molecular-machine-46l38xgcv7.pdf

The ATP Synthase—A Splendid Molecular Machine

Photonic bandgap crystals can reflect light for any direction of propagation in specific wavelength ranges1,2,3. This property, which can be used to confine, manipulate and guide photons, should allow the creation of all-optical integrated circuits. To achieve this goal, conventional semiconductor nanofabrication techniques have been adapted to make photonic crystals4,5,6,7,8,9. A potentially simpler and cheaper approach for creating three-dimensional periodic structures is the natural assembly of colloidal microspheres10,11,12,13,14,15. However, this approach yields irregular, polycrystalline photonic crystals that are difficult to incorporate into a device. More importantly, it leads to many structural defects that can destroy the photonic bandgap16,17. Here we show that by assembling a thin layer of colloidal spheres on a silicon substrate, we can obtain planar, single-crystalline silicon photonic crystals that have defect densities sufficiently low that the bandgap survives. As expected from theory, we observe unity reflectance in two crystalline directions of our photonic crystals around a wavelength of 1.3 micrometres. We also show that additional fabrication steps, intentional doping and patterning, can be performed, so demonstrating the potential for specific device applications.

On-chip natural assembly of silicon photonic bandgap crystals

The dynamics of two-dimensional ordering of micrometer-size polystyrene latex spheres on a horizontal glass substrate has been directly observed by means of optical microscopy. It turns out that the ordering starts when the thickness of the water layer containing particles becomes approximately equal to the particle diameter. By variation of the electrolyte concentration, the charge of the particles, and their volume fraction, it is proven that neither the electrostatic repulsion nor the van der Waals attraction between the particles is responsible for the formation of two-dimensional crystals. The direct observations revealed the main factors governing the ordering-the attractive capillary forces (due to the menisci formed around the particles) and the convective transport of particles toward the ordered region. The control of the water evaporation rate turns out to allow obtaining either well-ordered monolayers or well-ordered domains consisting of multilayers (bilayers, trilayers, etc.).

https://www.lcpe.uni-sofia.bg/publications/1992/pdf/1992-01-PK.pdf

Mechanism of formation of two-dimensional crystals from latex particles on substrates

/pdf/two-dimensional-crystallization-1vb1wohaca.pdf

Two-dimensional crystallization

http://www.k2.phys.waseda.ac.jp/PDF/1988BJ_KK_PulsedLM.pdf

Electroporation of cell membrane visualized under a pulsed-laser fluorescence microscope.

The iron storage protein, apoferritin, has a cavity in which iron is oxidized and stored as a hydrated oxide core. The size of the core is about 7 nm in diameter and is regulated by the cavity size. The cavity can be utilized as a nanoreactor to grow inorganic crystals. We incubated apoferritin in nickel or chromium salt solutions to fabricate hydroxide nanoparticles in the cavity. By using a solution containing dissolved carbon dioxide and by precisely controlling the pH, we succeeded in fabricating nickel and chromium cores. During the hydroxylation process of nickel ions a large portion of the apoferritin precipitated through bulk precipitation of nickel hydroxide. Bulk precipitation was suppressed by adding ammonium ions. However, even in the presence of ammonium ions the core did not form using a degassed solution. We concluded that carbonate ions were indispensable for core formation and that the ammonium ions prevented precipitation in the bulk solution. The optimized condition for nickel core formation was 0.3 mg/mL horse spleen apoferritin and 5 mM ammonium nickel sulfate in water containing dissolved carbon dioxide. The pH was maintained at 8.65 using two buffer solutions: 150 mM HEPES (pH 7.5) and 195 mM CAPSO (pH 9.5) with 20 mM ammonium at 23 degrees C. The pH had not changed after 48 h. After 24 h of incubation, all apoferritins remained in the supernatant and all of them had cores. Recombinant L-ferritin showed less precipitation even above a pH of 8.65. A chromium core was formed under the following conditions: 0.1 mg/mL apoferritin, 1 mM ammonium chromium sulfate, 100 mM HEPES (pH 7.5) with a solution containing dissolved carbon dioxide. About 80% of the supernatant apoferritin (0.07 mg/mL) formed a core. In nickel and chromium core formation, carbonate ions would play an important role in accelerating the hydroxylation in the apoferritin cavity compared to the bulk solution outside.

Fabrication of nickel and chromium nanoparticles using the protein cage of apoferritin

Cavities formed by proteins have been utilized as the reaction chamber for the fabrication of a range of inorganic nanoparticles, providing control of the size of particles by limiting growth and preventing agglomeration. In crystal form, proteins construct molecular arrays that can provide regularly arranged sites for nanoparticles. Here we report the fabrication of nanometric iron and indium particles using ferritin, an iron-storage protein. The indium nanoparticles thus formed have uniform spherical shape with diameter of 6.6 +/- 0.5 nm, while the iron nanoparticles are somewhat irregular in shape (5.8 +/- 1.0 nm). Regular two-dimensional arrays of these nanoparticles are successfully produced by crystallizing ferritin molecules on a water-air interface using the denatured protein film method. The lattice constant of these nanoparticle arrays is 13 nm with hexagonal packing, and arrays of more than 1 microm in area can be obtained by transfer onto silicon wafer.

Hideyuki Yoshimura

Papers

Mechanism of formation of two-dimensional crystals from latex particles on substrates

Two-dimensional crystallization

Electroporation of cell membrane visualized under a pulsed-laser fluorescence microscope.

Fabrication of nickel and chromium nanoparticles using the protein cage of apoferritin

Self-Organized Inorganic Nanoparticle Arrays on Protein Lattices