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  • 1.
    Möncke, Doris
    et al.
    Linnaeus University, Faculty of Technology, Department of Built Environment and Energy Technology. Alfred University, USA;Theoretical and Physical Chemistry Institute, Greece.
    Ali, Sharafat
    Linnaeus University, Faculty of Technology, Department of Built Environment and Energy Technology.
    Jonson, Bo
    Linnaeus University, Faculty of Technology, Department of Built Environment and Energy Technology.
    Kamitsos, Efstratios
    Theoretical and Physical Chemistry Institute, Greece.
    Anion polarizabilities in oxynitride glasses: Establishing a common optical basicity scale2020In: Physical Chemistry, Chemical Physics - PCCP, ISSN 1463-9076, E-ISSN 1463-9084Article in journal (Refereed)
    Abstract [en]

    Inspired by the work of John Duffy on optical basicity of oxyfluoride glasses, we apply here the conceptof optical basicity to oxynitride systems. While in the original work of Duffy and Ingram the basicity of amedium could be probed by s2 ions like Pb2+, the low energy intrinsic absorption edge of nitridecontainingsystems does not allow the use of such probe ions. This study uses therefore experimentaldata on refractive index and density of alkaline earth and rare earth containing silicate oxynitride glasses,prepared by the authors or taken from the literature. In addition, literature reports on experimental orcalculated refractive index, density and polarizability data are used to compare pure nitride systems, e.g.bulk or thin film materials that are either crystalline or glassy. We compare simple and complex nitridesystems with their oxygen counterparts, by calculating their optical basicity using the chemicalcomposition as well as the established relationship between optical basicity, L, and electronicpolarizability in oxide systems. Our results on oxynitride systems are in good agreement with Duffy’sprevious work on oxyfluoride glasses and indicate that the optical basicity varies for the isoelectronicanions in nitrides, oxides and fluorides (N3:O2:F) of a cation Mm+ as follows: L(MFm) = 1/2L(M2Om) =1/3L(M3Nm). Using this relation for CaO, for which the optical basicity was set as unity by Duffy andIngram, one has L(CaF2) = 0.50, L(CaO) = 1.00 and L(Ca3N2) = 1.50. The optical basicity of complexnitrides can therefore be calculated by the same method established for oxides using the equivalentfractions and the basicity of the constituent nitrides. The relationship between nitride polarizability aNand basicity L(nitride) was found to be linear, with L(nitride) = 0.39aN 0.14 where aN is given in Å3.

  • 2.
    Todde, Guido
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Friedman, Ran
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Conformational modifications induced by internal tandem duplications on the FLT3 kinase and juxtamembrane domains2019In: Physical Chemistry, Chemical Physics - PCCP, ISSN 1463-9076, E-ISSN 1463-9084, Vol. 21, no 34, p. 18467-18476Article in journal (Refereed)
    Abstract [en]

    he aberrant expression of FLT3 tyrosine kinase is associated primarily with acute myeloid leukaemia. This blood malignancy is often related to the onset of internal tandem duplications (ITDs) in the native sequence of the protein. The ITDs occur mainly in the juxtamembrane domain of the protein and alter the normal activity of the enzyme. In this work, we have studied the native form of FLT3 and six mutants by molecular dynamics simulations. The catalytic activity of FLT3 is exerted by the tyrosine kinase domain (KD) and regulated by the juxtamembrane (JM) domain. Analysis of the dynamics of these two domains have shown that the introduction of ITDs in the JM domain alters both structural and dynamic parameters. The presence of ITDs allowed the protein to span a larger portion of the conformational space, particularly in the JM domain and the activation loop. The FLT3 mutants were found to adopt more stable configurations than the native enzyme. This was due to the different arrangements assumed by the JM domain. Larger fluctuations of the activation loop were found in four of the six mutants. In the native FLT3, the key residue Tyr(572) is involved in a strong and stable interaction with an ion pair. This interaction, which is thought to keep the JM in place hence regulating the activity of the enzyme, was found to break in all FLT3 mutants.

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