Oscillating droplets by decomposition on the spherical harmonics basis.

In the framework of Rayleigh's description, we have investigated the eigenfrequencies of the capillary waves of a nonwetting droplet under forced oscillations (pointlike force). The theoretical model using the spherical harmonics Y(l,m)(theta, phi) as a part of the solution of the Laplace equation, is in good agreement with the experimental results. This model can be generalized for all kinds of excitations with a sitting or a levitating droplet due to the decomposition of the excitation on the spherical harmonics basis. From this study, a different theoretical way of interpreting droplet bouncing is presented motivating a wide range of industrial applications.

Chirality transfer and stereoselectivity of imprinted cholesteric networks.

Imprinting of cholesteric textures in a polymer network is a method of preserving a macroscopically chiral phase in a system with no molecular chirality. By modifying the elastic properties of the network, the resulting stored helical twist can be manipulated within a wide range since the imprinting efficiency depends on the balance between the elastic constants and twisting power at network formation. One spectacular property of phase chirality imprinting is the created ability of the network to adsorb preferentially one stereo component from a racemic mixture. In this paper we explore this property of chirality transfer from a macroscopic to a molecular scale. In particular, we focus on the competition between the phase chirality and the local nematic order. We demonstrate that it is possible to control the subsequent release of a chiral solvent component from the imprinting network and the reversibility of the stereo-selective swelling by racemic solvents.

Projection structure of a transcriptional regulator, HupR, determined by electron cryo-microscopy.

Large, well-ordered two-dimensional crystals of the histidine-tagged-HupR protein, a transcriptional regulator from the photosynthetic bacterium Rhodobacter capsulatus, were obtained by specific interaction with a Ni(2+)-chelated lipid monolayer. HupR is a response regulator of the NtrC subfamily; it activates the transcription of the structural genes hupSLC, of [NiFe]hydrogenase. A projection map of the full-length protein at 9 A resolution was obtained by electron cryo-microscopy and image analysis of frozen-hydrated two-dimensional crystals. The crystals have a p6 plane group with unit cell dimensions of a=b=111.6(+/-1.0) A, gamma=120.4(+/-0.5) degrees. The structure of the N-terminal domain of NtrC, the family to which HupR belongs, had been determined previously by NMR. The atomic coordinates of the N-terminal domain of NtrC, were compared to the structure obtained by cryo-electron microscope techniques of the whole HupR. These results provide the first structure at medium resolution of a whole transcription factor, HupR from the NtrC family.

Microcephaly and macrocephaly in autism.

Data from a series of 126 autistic children ages 2-16 years and referred to an Autism Diagnosis Unit in South-West France were examined. Macrocephaly (head circumference > 97th centile) was observed in 16.7% of the sample, a significantly higher proportion than that expected. Macrocephaly was more frequent among older subjects but was otherwise not associated with gender, developmental level, the presence of epilepsy or of medical disorders, or severity of autistic symptomatology. Microcephaly (head circumference < 3rd centile) was also significantly raised and found in 15.1% of the sample. Microcephaly was significantly associated with the presence of medical disorders. Results support those from recent studies suggesting a raised rate of macrocephaly in autism which, pooling published data, can be estimated to be 20%. It is argued that the raised incidence of microcephaly among low-functioning autistic subjects with medical disorders might have contributed to delay the recognition of an increased head circumference among a minority of subjects with idiopathic autism.

Induced helicity in biopolymer networks under stress.

By combining dynamic mechanical and optical measurements in probing the internal structure of a biopolymer network (gelatin gel), we studied the quasi-equilibrium evolution of helical content as a function of the applied stress. Assuming that the net optical activity is proportional to the concentration of secondary helices of collagen chains, and assuming that affine mechanical deformation, we find a nonmonotonic relationship between the helical domains and an imposed deformation. The results are in qualitative agreement with theoretical predictions of alpha-helices induced by chain end-to-end stretching, and give a consistent picture of mechanically stimulated helix-coil transition in networks of denatured polypeptides.

Stereo-selective swelling of imprinted cholesteric networks.

Molecular chirality, and the chiral symmetry breaking of resulting macroscopic phases, can be topologically imprinted and manipulated by cross-linking and swelling of polymer networks. We present a new experimental approach to stereo-specific separation of chiral isomers by using a cholesteric elastomer in which a helical director distribution has been topologically imprinted by cross-linking. This makes the material unusual in that is has a strong phase chirality, but no molecular chirality at all; we study the nature and parameters controlling the twist-untwist transition. Adding a racemic mixture to the imprinted network results in selective swelling by only the component of "correct" handedness. We investigate the capacity of demixing in a racemic environment, which depends on network parameters and the underlying nematic order.

Phase chirality and stereo-selective swelling of cholesteric elastomers.

Cholesteric elastomers possess a macroscopic "phase chirality" as the director n rotates in a helical fashion along an optical axis z and can be described by a chiral order parameter alpha. This parameter can be tuned by changing the helix pitch p and the elastic properties of the network at formation. The cholesterics also possess a local nematic order, changing with temperature or during solvent swelling. In this paper, by measuring the power of optical rotation d upsilon /dz , we discover how these two parameters vary as functions of temperature or solvent adsorbed by the network. The main result is a finding of pronounced stereo-selectivity of cholesteric elastomers, demonstrating itself in the retention of the "correct" chirality component of a racemic solvent. It has been possible to quantify the amount of such stereo-separation, and the basic dynamics of the effect.

Elasticity and plasticity of two-dimensional amorphous solid layers of beta-lactoglobulin.

We investigate the mechanical properties of a two-dimensional amorphous solid. It is formed spontaneously by the adsorption of a protein (the beta-lactoglobulin) at the surface of water. We measure its mechanical response in both elastic and plastic regimes by applying a point-like force (using a glass fiber). We compare our results with previous measurements of shear moduli using a floating torsion device.

Synchrotron radiation diffraction from two-dimensional protein crystals at the air/water interface.

Protein structure determination by classical x-ray crystallography requires three-dimensional crystals that are difficult to obtain for most proteins and especially for membrane proteins. An alternative is to grow two-dimensional (2D) crystals by adsorbing proteins to ligand-lipid monolayers at the surface of water. This confined geometry requires only small amounts of material and offers numerous advantages: self-assembly and ordering over micrometer scales is easier to obtain in two dimensions; although fully hydrated, the crystals are sufficiently rigid to be investigated by various techniques, such as electron crystallography or micromechanical measurements. Here we report structural studies, using grazing incidence synchrotron x-ray diffraction, of three different 2D protein crystals at the air-water interface, namely streptavidine, annexin V, and the transcription factor HupR. Using a set-up of high angular resolution, we observe narrow Bragg reflections showing long-range crystalline order in two dimensions. In the case of streptavidin the angular range of the observed diffraction corresponds to a resolution of 10 A in plane and 14 A normal to the plane. We show that this approach is complementary to electron crystallography but without the need for transfer of the monolayer onto a grid. Moreover, as the 2D crystals are accessible from the buffer solution, the formation and structure of protein complexes can be investigated in situ.