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Sökning: WFRF:(Benedikt Frank)

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1.
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2.
  • Boll, Rebecca, et al. (författare)
  • Imaging molecular structure through femtosecond photoelectron diffraction on aligned and oriented gas-phase molecules
  • 2014
  • Ingår i: Faraday Discussions. - : Royal Society of Chemistry (RSC). - 1364-5498. ; 171, s. 57-80
  • Tidskriftsartikel (refereegranskat)abstract
    • This paper gives an account of our progress towards performing femtosecond time-resolved photoelectron diffraction on gas-phase molecules in a pump-probe setup combining optical lasers and an X-ray free-electron laser. We present results of two experiments aimed at measuring photoelectron angular distributions of laser-aligned 1-ethynyl-4-fluorobenzene (C8H5F) and dissociating, laser-aligned 1,4-dibromobenzene (C6H4Br2) molecules and discuss them in the larger context of photoelectron diffraction on gas-phase molecules. We also show how the strong nanosecond laser pulse used for adiabatically laser-aligning the molecules influences the measured electron and ion spectra and angular distributions, and discuss how this may affect the outcome of future time-resolved photoelectron diffraction experiments.
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3.
  • Pimienta, Pierre, et al. (författare)
  • Recommendation of RILEM TC 256-SPF on fire spalling assessment during standardised fire resistance tests : complementary guidance and requirements
  • 2024
  • Ingår i: Materials and Structures/Materiaux et Constructions. - : Springer Science and Business Media B.V.. - 1359-5997 .- 1871-6873. ; 57:1
  • Tidskriftsartikel (refereegranskat)abstract
    • The recommendation is based on the co-authors’ work organized by the RILEM TC 256-SPF “Spalling of concrete due to fire: testing and modelling”. It aims to provide useful information, guidance and best practices in fire spalling assessment to laboratories that perform large-scale tests based on fire resistance test standards. It provides guidance on the spalling observation techniques during testing, as well as post-test spalling quantification/assessment methods. This document is intended to be used in conjunction with the fire resistance test standards, e.g. EN 1363-1 and ISO 834-1.
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4.
  • Pimienta, Pierre, et al. (författare)
  • Recommendation of RILEM TC 256-SPF on the method of testing concrete spalling due to fire : material screening test
  • 2023
  • Ingår i: Materials and Structures/Materiaux et Constructions. - : Springer Science and Business Media B.V.. - 1359-5997 .- 1871-6873. ; 56:9
  • Tidskriftsartikel (refereegranskat)abstract
    • The recommendation is based on the co-authors’ work organized by the RILEM TC 256-SPF “Spalling of concrete due to fire: testing and modelling”. The Committee has defined two types of screening tests for characterization of concrete propensity to fire spalling: Material screening tests and Product screening tests. Definitions of both types of tests are given in the paper. The following recommendations apply to Material screening tests. The material screening tests described in these recommendations are a set of minimum requirements to test concrete spalling propensity (for example, the minimal specimen size). This document covers the aspects of concrete characterization, specimen geometries, storage conditions, test methods and measured parameters.
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5.
  • Sohmen, Benedikt, et al. (författare)
  • The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90
  • 2023
  • Ingår i: Advanced Science. - : John Wiley & Sons. - 2198-3844. ; 10:36
  • Tidskriftsartikel (refereegranskat)abstract
    • Protein dynamics have been investigated on a wide range of time scales. Nano- and picosecond dynamics have been assigned to local fluctuations, while slower dynamics have been attributed to larger conformational changes. However, it is largely unknown how fast (local) fluctuations can lead to slow global (allosteric) changes. Here, fast molecule-spanning dynamics on the 100 to 200 ns time scale in the heat shock protein 90 (Hsp90) are shown. Global real-space movements are assigned to dynamic modes on this time scale, which is possible by a combination of single-molecule fluorescence, quasi-elastic neutron scattering and all-atom molecular dynamics (MD) simulations. The time scale of these dynamic modes depends on the conformational state of the Hsp90 dimer. In addition, the dynamic modes are affected to various degrees by Sba1, a co-chaperone of Hsp90, depending on the location within Hsp90, which is in very good agreement with MD simulations. Altogether, this data is best described by fast molecule-spanning dynamics, which precede larger conformational changes in Hsp90 and might be the molecular basis for allostery. This integrative approach provides comprehensive insights into molecule-spanning dynamics on the nanosecond time scale for a multi-domain protein.
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6.
  • Alessandro, B., et al. (författare)
  • Vector boson scattering : Recent experimental and theory developments
  • 2018
  • Ingår i: Reviews in Physics. - : Elsevier BV. - 2405-4283. ; 3, s. 44-63
  • Tidskriftsartikel (refereegranskat)abstract
    • This document summarises the talks and discussions happened during the VBSCan Split17 workshop, the first general meeting of the VBSCan COST Action network. This collaboration is aiming at a consistent and coordinated study of vector-boson scattering from the phenomenological and experimental point of view, for the best exploitation of the data that will be delivered by existing and future particle colliders. 
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7.
  • Aquila, Andrew, et al. (författare)
  • Time-resolved protein nanocrystallography using an X-ray free-electron laser
  • 2012
  • Ingår i: Optics Express. - 1094-4087. ; 20:3, s. 2706-2716
  • Tidskriftsartikel (refereegranskat)abstract
    • We demonstrate the use of an X-ray free electron laser synchronized with an optical pump laser to obtain X-ray diffraction snapshots from the photoactivated states of large membrane protein complexes in the form of nanocrystals flowing in a liquid jet. Light-induced changes of Photosystem I-Ferredoxin co-crystals were observed at time delays of 5 to 10 µs after excitation. The result correlates with the microsecond kinetics of electron transfer from Photosystem I to ferredoxin. The undocking process that follows the electron transfer leads to large rearrangements in the crystals that will terminally lead to the disintegration of the crystals. We describe the experimental setup and obtain the first time-resolved femtosecond serial X-ray crystallography results from an irreversible photo-chemical reaction at the Linac Coherent Light Source. This technique opens the door to time-resolved structural studies of reaction dynamics in biological systems.
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8.
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9.
  • Beck, Christian, et al. (författare)
  • Following Protein Dynamics in Real Time during Crystallization
  • 2019
  • Ingår i: Crystal Growth and Design. - : American Chemical Society (ACS). - 1528-7483 .- 1528-7505. ; , s. 7036-7045
  • Tidskriftsartikel (refereegranskat)abstract
    • The process of protein crystallization from aqueous protein solutions is still insufficiently understood. During macroscopic crystal formation, occurring often on time scales from a few hours to several days, protein dynamics evolves on the molecular level. Here, we present a proof of concept and a framework to observe this evolving diffusive dynamics on the pico- to nanosecond time scale, associated with cluster or precursor formation that ultimately results in emerging crystals. We investigated the model system of the protein β-lactoglobulin in D2O in the presence of ZnCl2, which induces crystallization by electrostatic bridges. First, the structural changes occurring during crystallization were followed by small-angle neutron scattering. Furthermore, we employed neutron backscattering and spin-echo spectroscopy to measure the ensemble-averaged self- and collective diffusion on nanosecond time scales of protein solutions with a kinetic time resolution on the order of 15 min. The experiments provide information on the increasing number fraction of immobilized proteins as well as on the diffusive motion of unbound proteins in an increasingly depleted phase. Simultaneously, information on the internal dynamics of the proteins is obtained.
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10.
  • Beck, Christian, et al. (författare)
  • Short-Time Transport Properties of Bidisperse Suspensions of Immunoglobulins and Serum Albumins Consistent with a Colloid Physics Picture.
  • 2022
  • Ingår i: Journal of Physical Chemistry B. - : American Chemical Society (ACS). - 1520-6106 .- 1520-5207. ; 126:38, s. 7400-7408
  • Tidskriftsartikel (refereegranskat)abstract
    • The crowded environment of biological systems such as the interior of living cells is occupied by macromolecules with a broad size distribution. This situation of polydispersity might influence the dependence of the diffusive dynamics of a given tracer macromolecule in a monodisperse solution on its hydrodynamic size and on the volume fraction. The resulting size dependence of diffusive transport crucially influences the function of a living cell. Here, we investigate a simplified model system consisting of two constituents in aqueous solution, namely, of the proteins bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig), systematically depending on the total volume fraction and ratio of these constituents. From high-resolution quasi-elastic neutron spectroscopy, the separate apparent short-time diffusion coefficients for BSA and Ig in the mixture are extracted, which show substantial deviations from the diffusion coefficients measured in monodisperse solutions at the same total volume fraction. These deviations can be modeled quantitatively using results from the short-time rotational and translational diffusion in a two-component hard sphere system with two distinct, effective hydrodynamic radii. Thus, we find that a simple colloid picture well describes short-time diffusion in binary mixtures as a function of the mixing ratio and the total volume fraction. Notably, the self-diffusion of the smaller protein BSA in the mixture is faster than the diffusion in a pure BSA solution, whereas the self-diffusion of Ig in the mixture is slower than in the pure Ig solution.
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