Littérature scientifique sur le sujet « ARTIFICIAL CELL, NMR, PROTEIN, FABP »
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Articles de revues sur le sujet "ARTIFICIAL CELL, NMR, PROTEIN, FABP"
GUTIÉRREZ-GONZÁLEZ, Luis H., Christian LUDWIG, Carsten HOHOFF, Martin RADEMACHER, Thorsten HANHOFF, Heinz RÜTERJANS, Friedrich SPENER et Christian LÜCKE. « Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP) ». Biochemical Journal 364, no 3 (15 juin 2002) : 725–37. http://dx.doi.org/10.1042/bj20020039.
Texte intégralHayakawa, Satoshi, Toshiisa Konishi, Tomohiko Yoshioka, Eiji Fujii et Kouji Kawabata. « NMR Structural Characterization of Mg-Containing Nano-Apatite ». Key Engineering Materials 631 (novembre 2014) : 57–60. http://dx.doi.org/10.4028/www.scientific.net/kem.631.57.
Texte intégralJuskewitz, Eric, Ekaterina Mishchenko, Vishesh K. Dubey, Marte Jenssen, Martin Jakubec, Philip Rainsford, Johan Isaksson, Jeanette H. Andersen et Johanna U. Ericson. « Lulworthinone : In Vitro Mode of Action Investigation of an Antibacterial Dimeric Naphthopyrone Isolated from a Marine Fungus ». Marine Drugs 20, no 5 (21 avril 2022) : 277. http://dx.doi.org/10.3390/md20050277.
Texte intégralAssante, G., A. Tourna, R. Carpani, F. Ferrari, D. Prati, F. Peyvandi, F. Blasi et al. « Reduced circulating FABP2 in patients with moderate to severe COVID-19 may indicate enterocyte functional change rather than cell death ». Scientific Reports 12, no 1 (5 novembre 2022). http://dx.doi.org/10.1038/s41598-022-23282-x.
Texte intégralThèses sur le sujet "ARTIFICIAL CELL, NMR, PROTEIN, FABP"
Perez, Santero Silvia. « Artificial Cells and Cell Mimics : Applications in Synthetic Biology and Biomolecular NMR Spectroscopy ». Doctoral thesis, 2016. http://hdl.handle.net/11562/939282.
Texte intégralSynthetic biology approaches usually develop cellular design using “bottom-up” strategies, inserting and deleting genes from existing organisms. Instead, “top-down” approaches could allow controlling living cells in a manner that does not require direct genetic modification. For example, artificial cells (laboratory-built cells, namely cell-like systems), can be used to “translate” external signals that the natural cells can “understand” without genetic modifications. Thus, we have developed artificial cellular mimics that send specific chemical messages to natural cells. These artificial cells inspired us another application aimed at understanding protein chemistry in cytomimetic systems. The complex cellular environment significantly modulates the behavior of macromolecules, affecting their structure, dynamics, and stability. Studies based on simplified cell mimics could provide important insights into protein chemistry in native-like environments. A distinctive feature of cellular systems is that the cytoplasmic medium is deeply crowded with significant concentrations of macromolecules (50-400 g/L) which affect several protein attributes (i.e. ligand binding, protein-protein interaction, folding, etc.). In this PhD thesis, two cytosolic, small, dynamic proteins were studied within an artificial cell environment by NMR Spectroscopy: human liver fatty acid binding protein (LFABP) and human ileal bile acid binding protein (IBABP), belonging to the intracellular lipid binding proteins (iLBPs). The crowded environment was mimicked by use of synthetic crowding agents (PEG, Ficoll or Dextran) and biomacromolecules (BSA, Lysozyme or Ubiquitin) in the range of concentrations 50-300 g/L. It was observed that Ficoll and/or Dextran are relatively inert. Instead, BSA and Lysozyme engaged in non-specific and specific interactions, respectively, with the test proteins. PEG interactions with proteins cannot be described quantitatively in terms of excluded volume alone and our results confirm the previous finding that PEG has tendency to interact with proteins. Moreover, also E. coli lysates and artificial cell systems such as water-in-oil emulsions and liposomes, were used to mimic the complex cellular environment and the restricted, lipid-bounded cytosolic milieu. In addition to structural and dynamic attributes, we investigated the lipid binding mechanism of LFABP under macromolecular crowding conditions.