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Sökning: WFRF:(Unger S.)

  • Resultat 151-160 av 175
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151.
  • Gopakumar, Geethanjali, et al. (författare)
  • X-ray-induced attosecond ion-water electron dynamics of aqueous ions
  • Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
    • The foundation of many physical and chemical processes is the transfer of charge from one entity to another. In many cases, the charge transfer is mediated by electron transfer and due to the comparatively low mass of electrons, these processes tend to take place within a few femtoseconds or several attoseconds. We investigate the charge transfer from Na+, Mg2+ and Al3+ in an aqueous environment to neighbouring water molecules. In order to achieve this, we use the core-hole clock method and Auger spectroscopy upon 1s ionization of the respective ions. The charge transfer times range from several 100 as below the 1s ionization threshold to only 20 as far above the 1s ionization. The decrease in charge transfer times as a function of the photon energy seems to be continuous. Despite the ions being isoelectronic in our study, we nd differences in their charge transfer behaviour.
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152.
  • Grimm, C. H., et al. (författare)
  • Selective extraction of small proteins from biological samples using a novel restricted access column with cation exchange properties
  • 2000
  • Ingår i: Chromatographia. - 0009-5893. ; 52:11-12, s. 703-709
  • Tidskriftsartikel (refereegranskat)abstract
    • The determination of proteins utilising a polymer-based restricted access support material with ion exchange properties (IERAM) is outlined. Solid phase extraction coupled on-line with a microbore reversed phase HPLC system for the quantitation of small marker proteins is demonstrated. The cation-exchange restricted access packings were characterised with respect to their adsorption and desorption kinetics. The IERAM material was also investigated by capacity, selectivity, and biocompatibility determinations when applied to the quantification of small molecular weight proteins such as cytochrome C, Lysozyme, Ribonuclease A, Myoglobin, Insulin, human serum albumin, and a Tryptic inhibitor. The integrated system was coupled to mass identity of selected proteins by MALDI-TOF mass spectrometry. The chromatographic outlet was interfaced to an "Interplate" fractionation collecter that sampled 1 μL volumes directly onto the MALDI target plate. The fully automated coupled column system was run unattended overnight and applied to protein quantitations in human plasma samples. Recovery data for a selected number of proteins varied between 90-96% (n = 10) with a limit of quantification around 2 μM with an injection volume of 100 μL. The RSD data were typically less than 8% at a 50 μM protein level (n = 7).
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153.
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156.
  • Johansson, Erik M. J., et al. (författare)
  • Efficient infiltration of low molecular weight polymer in nanoporous TiO2
  • 2011
  • Ingår i: Chemical Physics Letters. - : Elsevier BV. - 0009-2614 .- 1873-4448. ; 502:4-6, s. 225-230
  • Tidskriftsartikel (refereegranskat)abstract
    • The polymer APFO(3) was prepared with different molecular weights to study how the infiltration into nanoporous TiO2 films of different thickness depends on the size of the polymer. Also two different sizes of TiO2 nanoparticles were investigated to understand the effect of different pore size. It was observed that the lowest molecular weight polymer dissolved in chlorobenzene could infiltrate the nanoporous TiO2 network up to several micrometer thick films. It was concluded that efficient polymer infiltration into thick nanoporous layers was possible for the polymers with an estimated average chain length smaller than the diameter of the nanoparticles.
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157.
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158.
  • KjÊrvik, Marit, et al. (författare)
  • Comparative Study of NAP-XPS and Cryo-XPS for the Investigation of Surface Chemistry of the Bacterial Cell-Envelope
  • 2021
  • Ingår i: Frontiers in Chemistry. - : Frontiers Media S.A.. - 2296-2646. ; 9
  • Tidskriftsartikel (refereegranskat)abstract
    • Bacteria generally interact with the environment via processes involving their cell-envelope. Thus, techniques that may shed light on their surface chemistry are attractive tools for providing an understanding of bacterial interactions. One of these tools is Al Kα-excited photoelectron spectroscopy (XPS) with its estimated information depth of <10 nm. XPS-analyses of bacteria have been performed for several decades on freeze-dried specimens in order to be compatible with the vacuum in the analysis chamber of the spectrometer. A limitation of these studies has been that the freeze-drying method may collapse cell structure as well as introduce surface contaminants. However, recent developments in XPS allow for analysis of biological samples at near ambient pressure (NAP-XPS) or as frozen hydrated specimens (cryo-XPS) in vacuum. In this work, we have analyzed bacterial samples from a reference strain of the Gram-negative bacterium Pseudomonas fluorescens using both techniques. We compare the results obtained and, in general, observe good agreement between the two techniques. Furthermore, we discuss advantages and disadvantages with the two analysis approaches and the output data they provide. XPS reference data from the bacterial strain are provided, and we propose that planktonic cells of this strain (DSM 50090) are used as a reference material for surface chemical analysis of bacterial systems.
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