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The Global ETD Search service is a free service for researchers
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Showing 1 to 9 of 9 (0.035 seconds)Spelling suggestions: "subject:"proteolipid"" "subject:"proteolipids""
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Molecular and genetic analysis of the vha16 gene in Drosophila melanogasterGraham, Shirley January 2000 (has links)
No description available.
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Membrane Protein Folding: Modulating the Interactions between Transmembrane Alpha-helicesNg, Derek 13 January 2014 (has links)
The fundamental process by which an alpha-helical membrane protein attains its ultimate structure has previously been depicted as two energetically distinct stages where (1) the transmembrane (TM) segments are first threaded into the membrane bilayer as stable alpha-helices; and then (2) laterally interact to form the correct tertiary and/or quaternary structures. Central to the second stage of this model is the presence of amino acid sequence motifs in the TM segments that provide interaction-compatible surfaces through which the TM alpha-helices interact. Although these ideas have proven to be pivotal to the progress of the membrane protein folding field, a growing number of examples indicates that a variety of additional factors work together to dictate the ultimate interaction fate of TM embedded segments. In this context, we expand on these factors and explore other properties that can modulate the association of TM alpha-helices. A peptide model of myelin proteolipid protein (PLP) TM4 is capable of TM helix-helix interactions in SDS and biological membranes. Increasing the side chain volumes of two disease relevant residues (Ala242 and A248) reduces peptide self-association, indicating that these sites mediate TM helix packing through van der Waals interactions. Examination of the PLP TM2 alpha-helix shows that it is also capable of self-association and that its dimeric state depends on the presence or absence of residues at its C-terminus. Specifically, this sensitivity was attributed to changes in local hydrophobicity; a decrease in hydrophobicity likely reduces detergent-peptide interactions, which disrupts peptide alpha-helicity and the effectiveness of a nearby interaction compatible surface. We take advantage of this finding to determine the feasibility of coupling helix-helix interactions to an external factor such as pH. Our results indicate that pH can indeed modulate the dimerization state of the TM2 peptide and does so through the change in protonation state of Glu88. Increasing our knowledge of the variables contributing to TM helix-helix interactions provides valuable insights into membrane protein folding and how mutations can compromise this process. This knowledge will allow us to expand our arsenal of approaches to counter membrane protein misassembly--and ultimately human disease.
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Membrane Protein Folding: Modulating the Interactions between Transmembrane Alpha-helicesNg, Derek 13 January 2014 (has links)
The fundamental process by which an alpha-helical membrane protein attains its ultimate structure has previously been depicted as two energetically distinct stages where (1) the transmembrane (TM) segments are first threaded into the membrane bilayer as stable alpha-helices; and then (2) laterally interact to form the correct tertiary and/or quaternary structures. Central to the second stage of this model is the presence of amino acid sequence motifs in the TM segments that provide interaction-compatible surfaces through which the TM alpha-helices interact. Although these ideas have proven to be pivotal to the progress of the membrane protein folding field, a growing number of examples indicates that a variety of additional factors work together to dictate the ultimate interaction fate of TM embedded segments. In this context, we expand on these factors and explore other properties that can modulate the association of TM alpha-helices. A peptide model of myelin proteolipid protein (PLP) TM4 is capable of TM helix-helix interactions in SDS and biological membranes. Increasing the side chain volumes of two disease relevant residues (Ala242 and A248) reduces peptide self-association, indicating that these sites mediate TM helix packing through van der Waals interactions. Examination of the PLP TM2 alpha-helix shows that it is also capable of self-association and that its dimeric state depends on the presence or absence of residues at its C-terminus. Specifically, this sensitivity was attributed to changes in local hydrophobicity; a decrease in hydrophobicity likely reduces detergent-peptide interactions, which disrupts peptide alpha-helicity and the effectiveness of a nearby interaction compatible surface. We take advantage of this finding to determine the feasibility of coupling helix-helix interactions to an external factor such as pH. Our results indicate that pH can indeed modulate the dimerization state of the TM2 peptide and does so through the change in protonation state of Glu88. Increasing our knowledge of the variables contributing to TM helix-helix interactions provides valuable insights into membrane protein folding and how mutations can compromise this process. This knowledge will allow us to expand our arsenal of approaches to counter membrane protein misassembly--and ultimately human disease.
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Untersuchungen zur Stöchiometrie der Untereinheit c der ATP-Synthase aus Escherichia coliAldag, Ingo 26 June 2002 (has links)
Die mit der in dieser Arbeit entwickelten Rekonstitutionsmethode gemessenen Protonentranslokationsraten erreichen physiologisch relevante Werte und liegen ca. eine Größenordnung über Messungen, die mit vergleichbaren Methoden erzielt wurden. - Die Stöchiometrie der Untereinheit c ist in vitro vom Verhältnis der Untereinheiten a, b und c abhängig. Das bedeutet, dass bei einer Rekonstitution mit verringerter Menge an Untereinheit c Fo-Komplexe mit einheitlich weniger c-Untereinheiten entstehen. Das deutet darauf hin, dass der Fo-Komplex möglicherweise mit verschiedenen c-Stöchiometrien Protonen translozieren kann und dass die Stöchiometrie der Untereinheit c einen Einfluss auf die Protonentranslokationsrate des Fo-Komplexes haben könnte. - Die Stöchiometrie der Untereinheit c im FoF1-Komplex ist in vivo von der Expressionsrate ihres Gens weitgehend unabhängig. - Das unterschiedliche Verhalten der c-Stöchiometrie bei Variation der relativen c-Menge in vitro und in vivo legen einen Regulationsmechanismus in der Zelle nahe, der die Stöchiometrie der Untereinheit c je nach physiologischer Notwendigkeit einstellt und der unabhängig von der Expressionsrate der Untereinheit c arbeitet.
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Therapeutic approaches for two distinct CNS pathologiesStumpf, Sina Kristin 25 June 2018 (has links)
No description available.
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In vivo approach to myelin turnover and oligodendrocyte-dependent axonal integrityLüders, Katja 21 August 2018 (has links)
No description available.
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DISEASE MODELING AND THERAPEUTIC DEVELOPMENT FOR PELIZAEUS-MERZBACHER DISEASEElitt, Matthew S. 29 January 2019 (has links)
No description available.
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Characterization of the neuronal proteolipids M6A and M6B and the oligodendroglial tetraspans PLP and TSPAN2 in neural cell process formation / Charakterisierung der neuronalen Proteolipide M6A und M6B und der oligodendroglialen Viertransmembranproteine PLP und TSPAN2 in der Bildung von neuralen zellulären FortsätzenMonasterio Schrader, Patricia Irene de 20 July 2011 (has links)
No description available.
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Subcellular trafficking of proteolipid protein (PLP/DM20) and novel mechanisms of ER retention in Pelizaeus-Merzbacher disease / Subcellular trafficking of proteolipid protein (PLP/DM20) and novel mechanisms of ER retention in Pelizaeus-Merzbacher diseaseDhaunchak, Ajit Singh 26 June 2006 (has links)
No description available.
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