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Charge isomers of myelin basic protein: Structure and interactions with membranes, nucleotide analogues, and calmodulin
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.
Solar spectral conversion for improving the photosynthetic activity in algae reactors
2013, Wondraczek, L., Batentschuk, M., Schmidt, M.A., Borchardt, R., Scheiner, S., Seemann, B., Schweizer, P., Brabec, C.J.
Sustainable biomass production is expected to be one of the major supporting pillars for future energy supply, as well as for renewable material provision. Algal beds represent an exciting resource for biomass/biofuel, fine chemicals and CO2 storage. Similar to other solar energy harvesting techniques, the efficiency of algal photosynthesis depends on the spectral overlap between solar irradiation and chloroplast absorption. Here we demonstrate that spectral conversion can be employed to significantly improve biomass growth and oxygen production rate in closed-cycle algae reactors. For this purpose, we adapt a photoluminescent phosphor of the type Ca 0.59Sr0.40Eu0.01S, which enables efficient conversion of the green part of the incoming spectrum into red light to better match the Qy peak of chlorophyll b. Integration of a Ca 0.59Sr0.40Eu0.01S backlight converter into a flat panel algae reactor filled with Haematococcus pluvialis as a model species results in significantly increased photosynthetic activity and algae reproduction rate.