Symmetry breaking of ionic semiconductors under pressure: the case of InAs.

The NaCl-to-Cmcm phase transition and the Cmcm structure of InAs under high pressure are studied by x-ray diffraction. The lattice parameters and fractional coordinates are given as a function of pressure. We propose a mechanism responsible for this type of symmetry breaking under pressure. We show that the ppσ interactions do not play a major role in the stabilization of the NaCl structure. Consequently the NaCl-to-Cmcm transition occurs only in compounds with a large charge transfer. General conclusions on the behavior of III-V semiconductors under pressure are drawn.

A high-pressure structure in curium linked to magnetism.

Curium lies at the center of the actinide series and has a half-filled shell with seven 5f electrons spatially residing inside its radon core. As a function of pressure, curium exhibits five different crystallographic phases up to 100 gigapascals, of which all but one are also found in the preceding element, americium. We describe here a structure in curium, Cm III, with monoclinic symmetry, space group C2/c, found at intermediate pressures (between 37 and 56 gigapascals). Ab initio electronic structure calculations agree with the observed sequence of structures and establish that it is the spin polarization of curium's 5f electrons that stabilizes Cm III. The results reveal that curium is one of a few elements that has a lattice structure stabilized by magnetism.

Effect of the polar headgroup of phospholipids on their interaction with actin.

It is generally admitted that actin filaments are anchored to a membrane by membranar actin-binding-proteins. However, we found that actin may also interact directly with membrane phospholipids. The actin-phospholipid complex has been investigated at the air-water interface using a film balance technique. In order to probe the effect of the phospholipid headgroup on the actin-phospholipid interaction, we focus mainly on phospholipids that have the same acyl chain length but different headgroups. For all the phospholipids, the apparent area per molecule (the total surface divided by the number of lipid molecules) increases after the injection of the protein into the subphase, which suggests an intercalation of actin between the phospholipid molecules. This effect seems to be more important for DMPE and DMPS than for DMPG, suggesting that the headgroup plays an important role in this intercalation. The critical surface pressure associated to the liquid expanded-liquid condensed (LE-LC) phospholipid transition increases with the concentration of G-actin and thus suggests that G-actin acts as an impurity, simply competing as a surfactant at the air-water interface. On the other hand, F-actin affects the LE to LC transition of phospholipids differently. In this case, the LE to LC transition is broader and F-actin slightly decreases the critical surface pressure, which suggests that electrostatic interactions are involved.

Iron-silica interaction at extreme conditions and the electrically conducting layer at the base of Earth's mantle.

The boundary between the Earth's metallic core and its silicate mantle is characterized by strong lateral heterogeneity and sharp changes in density, seismic wave velocities, electrical conductivity and chemical composition. To investigate the composition and properties of the lowermost mantle, an understanding of the chemical reactions that take place between liquid iron and the complex Mg-Fe-Si-Al-oxides of the Earth's lower mantle is first required. Here we present a study of the interaction between iron and silica (SiO2) in electrically and laser-heated diamond anvil cells. In a multianvil apparatus at pressures up to 140 GPa and temperatures over 3,800 K we simulate conditions down to the core-mantle boundary. At high temperature and pressures below 40 GPa, iron and silica react to form iron oxide and an iron-silicon alloy, with up to 5 wt% silicon. At pressures of 85-140 GPa, however, iron and SiO2 do not react and iron-silicon alloys dissociate into almost pure iron and a CsCl-structured (B2) FeSi compound. Our experiments suggest that a metallic silicon-rich B2 phase, produced at the core-mantle boundary (owing to reactions between iron and silicate), could accumulate at the boundary between the mantle and core and explain the anomalously high electrical conductivity of this region.

Aggregate sound velocities and acoustic Grüneisen parameter of iron up to 300 GPa and 1,200 K.

Successful interpretation of available geophysical data requires experimental and theoretical information on the elasticity of solids under physical conditions of Earth's interior. Because iron is considered as major component in Earth's core, elastic properties of iron at high pressures and temperatures are very important for modeling its composition and dynamics. We use in situ x-ray diffraction data on epsilon-iron at static pressures up to 300 GPa and temperatures to 1,200 K to determine the Debye-Waller temperature factors and calculate aggregate sound velocities and Grüneisen parameter of epsilon-iron by using an approach that is based on Rietveld refinement at high pressures and temperatures.

Nanoflow gradient generator coupled with mu-LC-ESI-MS/MS for protein identification.

The large-scale identification of proteins from proteomes of complex organisms, and the availability of various types of protein and DNA databases, increasingly require the additional information provided by tandem mass spectrometry. HPLC and microLC coupled to ESI-MS/MS presently dominate the field of protein identification by tandem mass spectrometry and database searching. The analysis of protein digests is typically performed using HPLC or LC columns with 50-100-microm diameters, requiring the delivery of solvent gradients at low to mid nanoliter per minute flow rates. This has been typically achieved using expensive generic HPLC pumping systems for the delivery of microliter per minute gradients that were either flow-split or sampled. Here we present an alternative system for the delivery of nanoliter per minute gradients. The inexpensive nanoflow gradient generator (etagrad) described here can be modulated to reproducibly deliver selected gradients. The performance of the etagrad on-line with a microLC-ESI-MS/MS system has been demonstrated for the identification of standard protein digests. Moreover, the performance of the etagrad-microLC-ESI-MS/MS system, with protein prefractionation by IPG isoelectric focusing, was also evaluated for rapid study of yeast and human proteomes.

New delta (distorted-bcc) titanium to 220 GPa.

Structural phase transitions of a 3d transition element, titanium, have been investigated at pressures up to 220 GPa at room temperature using a monochromatic synchrotron x-ray diffraction technique. At 140 GPa, the hexagonal (omega) phase was transformed into an orthorhombic (delta) phase with a distorted bcc structure via an intermediate (gamma) phase, which has recently been proposed by Vohra and Spencer [Phys. Rev. Lett. 86, 3068 (2001)]. Both the delta and the gamma phases had a unique zigzag-chain-like structure, which resulted from an orthorhombic distortion. The delta-gamma transition could be explained as a rearrangement of the packing between the zigzag chains.

Stability of Ferropericlase in the Lower Mantle.

We have heated ferropericlases (Mg(0.60)Fe(0.40))O and (Mg(0.50)Fe(0.50))O to temperatures of 1000 kelvin at pressures of 86 gigapascals, simulating the stability of the solid solution at physical conditions relevant to Earth's lower mantle. The in situ x-ray study of the externally heated samples in a Mao-Bell-type diamond anvil cell shows that ferropericlase may dissociate into magnesium-rich and iron-rich oxide components. The result is important because the decomposition of ferropericlase into lighter and heavier phases will cause dynamic effects that could lead to mantle heterogeneity.

Determination of the secondary structure and conformation of puroindolines by infrared and Raman spectroscopy.

The conformation of puroindoline-a and -b, two basic lipid-binding proteins isolated from wheat seedlings, has been studied for the first time by infrared and Raman spectroscopy. The infrared results show that puroindoline-a and -b have similar secondary structure composed of approximately 30% alpha-helices, 30% beta-sheets, and 40% unordered structure at pH 7. The conformation of both puroindolines is significantly pH-dependent. The reduction of the disulfide bridges leads to a decrease of the solubility of puroindolines in water and to an increase of the beta-sheet content by about 15% at the expense of the alpha-helix content. Raman spectroscopy confirms the structure similarity between the two puroindolines with little differences in the side chains' environment. All the disulfide bridges are in a gauche-gauche-gauche conformation, and the unique tyrosine residue present in both puroindolines is hydrogen-bonded to water. Raman spectra have been recorded in both H2O and D2O media, thus providing additional information concerning the accessibility of certain residues to water. We have also observed that puroindoline-a tends to form some aggregates under acidic and high ionic strength conditions. Near-ultraviolet circular dichroism measurements suggest that the tryptophan-rich domain is involved in this aggregate formation. Finally, on the basis of a combined infrared and sequence conformational analysis, we propose a secondary structure assignment for both puroindolines. The results show that puroindolines exhibit a similar folding pattern with plant nonspecific lipid-transfer protein and some amylase-protease inhibitors. These proteins could form a homogeneous structural family of plant proteins involved in the defense against pathogens that are probably derived from a common "helicoidal" protein ancestor.

Kinetic study of the thermal denaturation of G actin using differential scanning calorimetry and intrinsic fluorescence spectroscopy.

Previous studies of the thermal denaturation of G actin have yielded conflicting results which have led to contradictory interpretations of the denaturation process. In their interpretations, these authors postulated that the thermal denaturation of G actin can be described by thermodynamical equilibrium laws despite the fact that this transition is irreversible. Using differential scanning calorimetry and fluorescence spectroscopy, we now show that thermal denaturation of G actin does not obey to equilibrium thermodynamics, but rather, is a two-step irreversible phenomenon under kinetic control. It can therefore be analyzed using the recently developed Sanchez-Ruiz equations.

Stabilization of actin by phalloidin: a differential scanning calorimetric study.

We have used differential scanning calorimetry to study the effects of phalloidin on F and G actin stability. For F actin, saturating concentrations of phalloidin induced an important shift on the transition temperature, Tm, from 69.5 degrees C to 83.5 degrees C. However, the calorimetric enthalpy remained unchanged. Using lower phalloidin concentrations, monomers linked to phalloidin, as well as neighboring unlinked monomers, were both stabilized. Contrary to previous reports, phalloidin was also shown to affect G actin, shifting its Tm from 59.5 degrees C to 75 degrees C. Two mechanisms are proposed to explain this finding: first, it could indicate a real interaction of phalloidin with G actin, and second, heating of the specimen during the scan could have induced polymerization of some G actin to the F form. The resulting F polymer would then interact with phalloidin, thus shifting the equilibrium between G and F actin towards the polymeric form.