25 research outputs found
Measurement of event-shape observables in Z→ℓ+ℓ− events in pp collisions at √ s=7 TeV with the ATLAS detector at the LHC
Event-shape observables measured using charged particles in inclusive
-boson events are presented, using the electron and muon decay modes of the
bosons. The measurements are based on an integrated luminosity of of proton--proton collisions recorded by the ATLAS detector at the
LHC at a centre-of-mass energy TeV. Charged-particle
distributions, excluding the lepton--antilepton pair from the -boson decay,
are measured in different ranges of transverse momentum of the boson.
Distributions include multiplicity, scalar sum of transverse momenta, beam
thrust, transverse thrust, spherocity, and -parameter, which are
in particular sensitive to properties of the underlying event at small values
of the -boson transverse momentum. The Sherpa event generator shows larger
deviations from the measured observables than Pythia8 and Herwig7. Typically,
all three Monte Carlo generators provide predictions that are in better
agreement with the data at high -boson transverse momenta than at low
-boson transverse momenta and for the observables that are less sensitive to
the number of charged particles in the event.Comment: 36 pages plus author list + cover page (54 pages total), 14 figures,
4 tables, submitted to EPJC, All figures including auxiliary figures are
available at
http://atlas.web.cern.ch/Atlas/GROUPS/PHYSICS/PAPERS/STDM-2014-0
Structural and Functional Role of the Disulfide Bridges in the Hydrophobin SC3
Hydrophobins function in fungal development by self-assembly at hydrophobic-hydrophilic interfaces such as the interface between the fungal cell wall and the air or a hydrophobic solid. These proteins contain eight conserved cysteine residues that form four disulfide bonds. To study the effect of the disulfide bridges on the self-assembly, the disulfides of the SC3 hydrophobin were reduced with 1,4-dithiothreitol. The free thiols were then blocked with either iodoacetic acid (IAA) or iodoacetamide (IAM), introducing eight or zero negative charges, respectively. Circular dichroism and infrared spectroscopy showed that after opening of the disulfide bridges SC3 is initially unfolded. IAA-SC3 did not self-assemble at the air-water interface upon shaking an aqueous solution. Remarkably, after drying down IAA-SC3 or after exposing it to Teflon, it refolded into a structure similar to that observed for native SC3 at these interfaces. Iodoacetamide-SC3 on the other hand, which does not contain extra charges, spontaneously refolded in water in the amyloid-like β-sheet conformation, characteristic for SC3 assembled at the water-air interface. From this we conclude that the disulfide bridges of SC3 are not directly involved in self-assembly but keep hydrophobin monomers soluble in the fungal cell or its aqueous environment, preventing premature self-assembly.
Self-assembly of the hydrophobin SC3 proceeds via two structural intermediates
Hydrophobins self assemble into amphipathic films at hydrophobic–hydrophilic interfaces. These proteins are involved in a broad range of processes in fungal development. We have studied the conformational changes that accompany the self-assembly of the hydrophobin SC3 with polarization-modulation infrared reflection absorption spectroscopy, attenuated total reflection Fourier transform infrared spectroscopy, and circular dichroism, and related them to changes in morphology as observed by electron microcopy. Three states of SC3 have been spectroscopically identified previously as follows: the monomeric state, the α-helical state that is formed upon binding to a hydrophobic solid, and the β-sheet state, which is formed at the air–water interface. Here, we show that the formation of the β-sheet state of SC3 proceeds via two intermediates. The first intermediate has an infrared spectrum indistinguishable from that of the α-helical state of SC3. The second intermediate is rich in β-sheet structure and has a featureless appearance under the electron microscope. The end state has the same secondary structure, but is characterized by the familiar 10-nm-wide rodlets