Active self-assembly of colloidal machines with passive rotational parts coordination of phoresis and osmosis.

The organization of microscopic objects into specific structures with movable parts is a prerequisite for building sophisticated micromachines with complex functions, as exemplified by their macroscopic counterparts. Here we report the self-assembly of active and passive colloids into micromachinery with passive rotational parts. Depending on the attachment of the active colloid to a substrate, which varies the degrees of free freedom of the assembly, colloidal machines with rich internal rotational dynamics are realized.

Design and One-Pot Synthesis of Capsid-like Gold Colloids with Tunable Surface Roughness and Their Enhanced Sensing and Catalytic Performances.

Viral capsid-like particles tiled with mosaic patches have attracted great attention as they imitate nature's design to achieve advanced material properties and functions. Here, we develop a facile one-pot soft-template method to synthesize biomimetic gold capsid-like colloids with tunable particle size and surface roughness. Uniform submicron-to-micron-sized hollow gold colloidal particles are successfully achieved by using tannic acids as soft templates and reducing agents, which first self-assemble into spherical complex templates before the reduction of Au ions via their surface hydroxyl groups.

Identification of allosteric disulfides from prestress analysis.

Disulfide bonds serve to form physical cross-links between residues in protein structures, thereby stabilizing the protein fold. Apart from this purely structural role, they can also be chemically active, participating in redox reactions, and they may even potentially act as allosteric switches controlling protein functions. Specific types of disulfide bonds have been identified in static protein structures from their distinctive pattern of dihedral bond angles, and the allosteric function of such bonds is purported to be related to the torsional strain they store.

Force distribution analysis of mechanochemically reactive dimethylcyclobutene.

Internal molecular forces can guide chemical reactions, yet are not straightforwardly accessible within a quantum mechanical description of the reacting molecules. Here, we present a force-matching force distribution analysis (FM-FDA) to analyze internal forces in molecules. We simulated the ring opening of trans-3,4-dimethylcyclobutene (tDCB) with on-the-fly semiempirical molecular dynamics.

How fast does a signal propagate through proteins?

As the molecular basis of signal propagation in the cell, proteins are regulated by perturbations, such as mechanical forces or ligand binding. The question arises how fast such a signal propagates through the protein molecular scaffold. As a first step, we have investigated numerically the dynamics of force propagation through a single (Ala)[Formula: see text] protein following a sudden increase in the stretching forces applied to its end termini.

Isopeptide bonds mechanically stabilize spy0128 in bacterial pili.

Pili on the surface of Streptococcus pyogenes play a crucial role in adhesion to and colonization in human cells. The major pilin subunit, Spy0128, features intramolecular covalent isopeptide bonds that autocatalytically form between the side chains of lysine and asparagine residues and are regarded as important factors in conveying structural stability. In support of this notion, single-molecule force spectroscopy experiments with Spy0128 recently demonstrated the inextensibility of these bonds under mechanical load.

On the cis to trans isomerization of prolyl-peptide bonds under tension.

The cis peptide bond is a characteristic feature of turns in protein structures and can play the role of a hinge in protein folding. Such cis conformations are most commonly found at peptide bonds immediately preceding proline residues, as the cis and trans states for such bonds are close in energy. However, isomerization over the high rotational barrier is slow.

Dynamic prestress in a globular protein.

A protein at equilibrium is commonly thought of as a fully relaxed structure, with the intra-molecular interactions showing fluctuations around their energy minimum. In contrast, here we find direct evidence for a protein as a molecular tensegrity structure, comprising a balance of tensed and compressed interactions, a concept that has been put forward for macroscopic structures. We quantified the distribution of inter-residue prestress in ubiquitin and immunoglobulin from all-atom molecular dynamics simulations.

Glycosylation enhances peptide hydrophobic collapse by impairing solvation.

Post-translational N-glycosylation of proteins is ubiquitous in eukaryotic cells, and has been shown to influence the thermodynamics of protein collapse and folding. However, the mechanism for this influence is not well understood. All-atom molecular dynamics simulations are carried out to study the collapse of a peptide linked to a single N-glycan.

Effects of internal flow and viscosity ratio on measurements of dynamic forces between deformable drops.

A model that has been shown to give very accurate predictions of dynamic forces between deformable emulsion drops and bubbles is used to quantify the effects of internal flow and viscosity ratio on the hydrodynamic interaction in such systems. The results demonstrate that direct force measurement using an atomic force microscope can readily differentiate whether the interfaces of drops of different viscosities respond as immobile (no-slip) or fully mobile (no tangential shear stress) boundaries.

Measurements of dynamic forces between drops with the AFM: novel considerations in comparisons between experiment and theory.

Dynamic forces between a deformable tetradecane oil drop (radius of curvature ≈ 25 μm) anchored on the cantilever of the Atomic Force Microscope (AFM) and similar oil drops (radii of curvature 80 to 500 μm) on the substrate in aqueous electrolyte with added sodium dodecyl sulfate surfactant have been studied. Measurements were made over a range of scan rates that span the range of Brownian velocities of such emulsion drops. The adsorbed anionic surfactants impart a stabilising electrical double layer repulsion between the drops so coalescence was not observed under present conditions.

Atomic force microscopy: loading position dependence of cantilever spring constants and detector sensitivity.

A simple and accurate experimental method is described for determining the effective cantilever spring constant and the detector sensitivity of atomic force microscopy cantilevers on which a colloidal particle is attached. By attaching large (approximately 85 microm diameter) latex particles at various positions along the V-shaped cantilevers, we demonstrate how the normal and lateral spring constants as well as the sensitivity vary with loading position. Comparison with an explicit point-load theoretical model has also been used to verify the accuracy of the method.