Monochromatic trees in random tournaments

We prove that, with high probability, in every 2-edge-colouring of the random tournament on n vertices there is a monochromatic copy of every oriented tree of order O(n/ \sqrt{log n}. This generalizes a result of the first, third and fourth authors, who proved the same statement for paths, and is tight up to a constant factor

Four-dimensional light shaping: manipulating ultrafast spatio-temporal foci in space and time

Spectral dispersion of ultrashort pulses allows simultaneous focusing of light in both space and time creating so-called spatio-temporal foci. Such space-time coupling may be combined with existing holographic techniques to give a further dimension of control when generating focal light fields. It is shown that a phase-only hologram placed in the pupil plane of an objective and illuminated by a spatially chirped ultrashort pulse can be used to generate three dimensional arrays of spatio-temporally focused spots. Exploiting the pulse front tilt generated at focus when applying simultaneous spatial and temporal focusing (SSTF), it is possible to overlap neighbouring foci in time to create a smooth intensity distribution. The resulting light field displays a high level of axial confinement, with experimental demonstrations given through two-photon microscopy and non-linear laser fabrication of glass

SEMENTEIRO: Multiplicação de batatasemente para uso próprio.

bitstream/item/31441/1/comunicado-207.pd

Aureochrome 1 illuminated: structural changes of a transcription factor probed by molecular spectroscopy.

Aureochrome 1 from Vaucheria frigida is a recently identified blue-light receptor that acts as a transcription factor. The protein comprises a photosensitive light-, oxygen- and voltage-sensitive (LOV) domain and a basic zipper (bZIP) domain that binds DNA rendering aureochrome 1 a prospective optogenetic tool. Here, we studied the photoreaction of full-length aureochrome 1 by molecular spectroscopy. The kinetics of the decay of the red-shifted triplet state and the blue-shifted signaling state were determined by time-resolved UV/Vis spectroscopy. It is shown that the presence of the bZIP domain further prolongs the lifetime of the LOV390 signaling state in comparison to the isolated LOV domain whereas bound DNA does not influence the photocycle kinetics. The light-dark Fourier transform infrared (FTIR) difference spectrum shows the characteristic features of the flavin mononucleotide chromophore except that the S-H stretching vibration of cysteine 254, which is involved in the formation of the thio-adduct state, is significantly shifted to lower frequencies compared to other LOV domains. The presence of the target DNA influences the light-induced FTIR difference spectrum of aureochrome 1. Vibrational bands that can be assigned to arginine and lysine side chains as well to the phosphate backbone, indicate crucial changes in interactions between transcription factor and DNA

Traces of stimulated bosonic exciton-scattering in semiconductor luminescence

We observe signatures of stimulated bosonic scattering of excitons, a precursor of Bose-Einstein-Condensation (BEC), in the photoluminescence of semiconductor quantum wells. The optical decay of a spinless molecule of two excitons (biexciton) into an exciton and a photon with opposite angular momenta is subject to bosonic enhancement in the presence of other excitons. In a spin polarized gas of excitons the bosonic enhancement breaks the symmetry of two equivalent decay channels leading to circularly polarized luminescence of the biexciton with the sign opposite to the excitonic luminescence. Comparison of experiment and many body theory proves stimulated scattering of excitons, but excludes the presence of a fully condensed BEC-like state.Comment: 5 page

Resonance Raman and FTIR spectroscopic characterization of the closed and open states of channelrhodopsin-1.

Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) is a light-activated cation channel, which is a promising optogenetic tool. We show by resonance Raman spectroscopy and retinal extraction followed by high pressure liquid chromatography (HPLC) that the isomeric ratio of all-trans to 13-cis of solubilized channelrhodopsin-1 is with 70:30 identical to channelrhodopsin-2 from Chlamydomonas reinhardtii (CrChR2). Critical frequency shifts in the retinal vibrations are identified in the Raman spectrum upon transition to the open (conductive P2(380)) state. Fourier transform infrared spectroscopy (FTIR) spectra indicate different structures of the open states in the two channelrhodopsins as reflected by the amide I bands and the protonation pattern of acidic amino acids

In-Situ Observation of Membrane Protein Folding during Cell-Free Expression.

Proper insertion, folding and assembly of functional proteins in biological membranes are key processes to warrant activity of a living cell. Here, we present a novel approach to trace folding and insertion of a nascent membrane protein leaving the ribosome and penetrating the bilayer. Surface Enhanced IR Absorption Spectroscopy selectively monitored insertion and folding of membrane proteins during cell-free expression in a label-free and non-invasive manner. Protein synthesis was performed in an optical cell containing a prism covered with a thin gold film with nanodiscs on top, providing an artificial lipid bilayer for folding. In a pilot experiment, the folding pathway of bacteriorhodopsin via various secondary and tertiary structures was visualized. Thus, a methodology is established with which the folding reaction of other more complex membrane proteins can be observed during protein biosynthesis (in situ and in operando) at molecular resolution

2s Hyperfine Structure in Hydrogen Atom and Helium-3 Ion

The usefulness of study of hyperfine splitting in the hydrogen atom is limited on a level of 10 ppm by our knowledge of the proton structure. One way to go beyond 10 ppm is to study a specific difference of the hyperfine structure intervals 8 Delta nu_2 - Delta nu_1. Nuclear effects for are not important this difference and it is of use to study higher-order QED corrections.Comment: 10 pages, presented at Hydrogen Atom II meeting (2000

Active Membrane Fluctuations Studied by Micropipet Aspiration

We present a detailed analysis of the micropipet experiments recently reported in J-B. Manneville et al., Phys. Rev. Lett. 82, 4356--4359 (1999), including a derivation of the expected behaviour of the membrane tension as a function of the areal strain in the case of an active membrane, i.e., containing a nonequilibrium noise source. We give a general expression, which takes into account the effect of active centers both directly on the membrane, and on the embedding fluid dynamics, keeping track of the coupling between the density of active centers and the membrane curvature. The data of the micropipet experiments are well reproduced by the new expressions. In particular, we show that a natural choice of the parameters quantifying the strength of the active noise explains both the large amplitude of the observed effects and its remarkable insensitivity to the active-center density in the investigated range. [Submitted to Phys Rev E, 22 March 2001]Comment: 14 pages, 5 encapsulated Postscript figure

Molecular details of the unique mechanism of chloride transport by acyanobacterial rhodopsin

Microbial rhodopsins are well known as versatile and ubiquitous light-driven ion transporters and photosensors. While the proton transport mechanism has been studied in great detail, much less is known about various modes of anion transport. Until recently, only two main groups of light-driven anion pumps were known, archaeal halorhodopsins (HRs) and bacterial chloride pumps (known as ClRs or NTQs). Last year, another group of cyanobacterial anion pumps with a very distinct primary structure was reported. Here, we studied the chloride- transporting photocycle of a representative of this new group, Mastigocladopsis repens rhodopsin (MastR), using time-resolved spectroscopy in the infrared and visible ranges and site-directed mutagenesis. We found that, in accordance with its unique amino acid sequence containing many polar residues in the transmembrane region of the protein, its photocycle features a number of unusual molecular events not known for other anion-pumping rhodopsins. It appears that light-driven chloride ion transfers by MastR are coupled with translocation of protons and water molecules as well as perturbation of several polar sidechains. Of particular interest is transient deprotonation of Asp-85, homologous to the cytoplasmic proton donor of light- driven proton pumps (such as Asp-96 of bacteriorhodopsin), which may serve as a regulatory mechanism