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Subject: article × Subject: chemistry × WGL Institute: IPHT ×

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    Volume fraction determination of binary liquid mixtures by measurement of the equalization wavelength
    (Basel : MDPI, 2010) Martincek, I.; Pudis, D.; Kacik, D.; Schuster, K.
    A method for determination of the volume fraction in binary liquid mixtures by measurement of the equalization wavelength of intermodal interference of modes LP01 and LP11 in a liquid core optical fiber is presented in this paper. This method was studied using a liquid core optical fiber with fused silica cladding and a core made up of a binary silicon oil/chloroform liquid mixture with different volume fractions of chloroform. The interference technique used allows us to determine the chloroform volume fraction in the binary mixture with accuracy better than 0.1%. One of the most attractive advantages of presented method is very small volume of investigated mixture needed, as only a few hundred picoliters are necessary for reliable results. © 2010 by the authors.
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    Local protonation control using plasmonic activation
    (Cambridge : RSC, 2001) Singh, P.; Deckert, V.
    Localized protonation of 4-mercaptopyridine (4-MPY), activated by light in the presence of silver nanoparticles is monitored under ambient conditions using surface-enhanced Raman scattering (SERS) and tip-enhanced Raman scattering (TERS). The reaction can be controlled by the excitation wavelength and the atmospheric conditions, thus, providing a tool for site-specific control of protonation.
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    Charge isomers of myelin basic protein: Structure and interactions with membranes, nucleotide analogues, and calmodulin
    (San Francisco, CA : Public Library of Science, 2011) Wang, C.; Neugebauer, U.; Bürck, J.; Myllykoski, M.; Baumgärtel, P.; Popp, J.; Kursula, P.
    As an essential structural protein required for tight compaction of the central nervous system myelin sheath, myelin basic protein (MBP) is one of the candidate autoantigens of the human inflammatory demyelinating disease multiple sclerosis, which is characterized by the active degradation of the myelin sheath. In this work, recombinant murine analogues of the natural C1 and C8 charge components (rmC1 and rmC8), two isoforms of the classic 18.5-kDa MBP, were used as model proteins to get insights into the structure and function of the charge isomers. Various biochemical and biophysical methods such as size exclusion chromatography, calorimetry, surface plasmon resonance, small angle X-ray and neutron scattering, Raman and fluorescence spectroscopy, and conventional as well as synchrotron radiation circular dichroism were used to investigate differences between these two isoforms, both from the structural point of view, and regarding interactions with ligands, including calmodulin (CaM), various detergents, nucleotide analogues, and lipids. Overall, our results provide further proof that rmC8 is deficient both in structure and especially in function, when compared to rmC1. While the CaM binding properties of the two forms are very similar, their interactions with membrane mimics are different. CaM can be used to remove MBP from immobilized lipid monolayers made of synthetic lipids - a phenomenon, which may be of relevance for MBP function and its regulation. Furthermore, using fluorescently labelled nucleotides, we observed binding of ATP and GTP, but not AMP, by MBP; the binding of nucleoside triphosphates was inhibited by the presence of CaM. Together, our results provide important further data on the interactions between MBP and its ligands, and on the differences in the structure and function between MBP charge isomers.