Two-dimensional shear modulus of a Langmuir foam

We deform a two-dimensional (2D) foam, created in a Langmuir monolayer, by applying a mechanical perturbation, and simultaneously image it by Brewster angle microscopy. We determine the foam stress tensor (through a determination of the 2D gas-liquid line tension, 2.35 $\pm$ 0.4 pJ$\cdot$m$^{-1}$) and the statistical strain tensor, by analyzing the images of the deformed structure. We deduce the 2D shear modulus of the foam, $\mu= 38 \pm 3 \mathrm{nN}\cdot \mathrm{m}^{-1}$. The foam effective rigidity is predicted to be $35 \pm 3 \mathrm {nN}\cdot \mathrm {m}^{- 1}$, which agrees with the value $37.5 \pm 0.8 \mathrm {nN}\cdot \mathrm {m}^{-1}$ obtained in an independent mechanical measurement.Comment: submitted May 12, 2003 ; resubmitted Sept 9, 200

Ferromagnetism in Oriented Graphite Samples

We have studied the magnetization of various, well characterized samples of highly oriented pyrolitic graphite (HOPG), Kish graphite and natural graphite to investigate the recently reported ferromagnetic-like signal and its possible relation to ferromagnetic impurities. The magnetization results obtained for HOPG samples for applied fields parallel to the graphene layers - to minimize the diamagnetic background - show no correlation with the magnetic impurity concentration. Our overall results suggest an intrinsic origin for the ferromagnetism found in graphite. We discuss possible origins of the ferromagnetic signal.Comment: 11 figure

Two-sided Grassmann-Rayleigh quotient iteration

The two-sided Rayleigh quotient iteration proposed by Ostrowski computes a pair of corresponding left-right eigenvectors of a matrix $C$. We propose a Grassmannian version of this iteration, i.e., its iterates are pairs of $p$-dimensional subspaces instead of one-dimensional subspaces in the classical case. The new iteration generically converges locally cubically to the pairs of left-right $p$-dimensional invariant subspaces of $C$. Moreover, Grassmannian versions of the Rayleigh quotient iteration are given for the generalized Hermitian eigenproblem, the Hamiltonian eigenproblem and the skew-Hamiltonian eigenproblem.Comment: The text is identical to a manuscript that was submitted for publication on 19 April 200

Mixed exciton–charge-transfer states in photosystem II: Stark spectroscopy on site–directed mutants

AbstractWe investigated the electronic structure of the photosystem II reaction center (PSII RC) in relation to the light-induced charge separation process using Stark spectroscopy on a series of site-directed PSII RC mutants from the cyanobacterium Synechocystis sp. PCC 6803. The site-directed mutations modify the protein environment of the cofactors involved in charge separation (PD1, PD2, ChlD1, and PheD1). The results demonstrate that at least two different exciton states are mixed with charge-transfer (CT) states, yielding exciton states with CT character: (PD2δ+PD1δ−ChlD1)∗673nm and (ChlD1δ+PheD1δ−)∗681nm (where the subscript indicates the wavelength of the electronic transition). Moreover, the CT state PD2+PD1− acquires excited-state character due to its mixing with an exciton state, producing (PD2+PD1−)δ∗684nm. We conclude that the states that initiate charge separation are mixed exciton-CT states, and that the degree of mixing between exciton and CT states determines the efficiency of charge separation. In addition, the results reveal that the pigment-protein interactions fine-tune the energy of the exciton and CT states, and hence the mixing between these states. This mixing ultimately controls the selection and efficiency of a specific charge separation pathway, and highlights the capacity of the protein environment to control the functionality of the PSII RC complex

Membrane Association of the PTEN Tumor Suppressor: Molecular Details of the Protein-Membrane Complex from SPR Binding Studies and Neutron Reflection

The structure and function of the PTEN phosphatase is investigated by studying its membrane affinity and localization on in-plane fluid, thermally disordered synthetic membrane models. The membrane association of the protein depends strongly on membrane composition, where phosphatidylserine (PS) and phosphatidylinositol diphosphate (PI(4,5)P2) act pronouncedly synergistic in pulling the enzyme to the membrane surface. The equilibrium dissociation constants for the binding of wild type (wt) PTEN to PS and PI(4,5)P2 were determined to be Kd∼12 µM and 0.4 µM, respectively, and Kd∼50 nM if both lipids are present. Membrane affinities depend critically on membrane fluidity, which suggests multiple binding sites on the protein for PI(4,5)P2. The PTEN mutations C124S and H93R show binding affinities that deviate strongly from those measured for the wt protein. Both mutants bind PS more strongly than wt PTEN. While C124S PTEN has at least the same affinity to PI(4,5)P2 and an increased apparent affinity to PI(3,4,5)P3, due to its lack of catalytic activity, H93R PTEN shows a decreased affinity to PI(4,5)P2 and no synergy in its binding with PS and PI(4,5)P2. Neutron reflection measurements show that the PTEN phosphatase “scoots" along the membrane surface (penetration <5 Å) but binds the membrane tightly with its two major domains, the C2 and phosphatase domains, as suggested by the crystal structure. The regulatory C-terminal tail is most likely displaced from the membrane and organized on the far side of the protein, ∼60 Å away from the bilayer surface, in a rather compact structure. The combination of binding studies and neutron reflection allows us to distinguish between PTEN mutant proteins and ultimately may identify the structural features required for membrane binding and activation of PTEN