müllar stefan (5 resultados)

Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The function of membrane proteins is mainly dependend on their aggregational behavior. Some are active as monomers, whereas others need to assemble into oligomeric states.1 In this context, molecular recognition, which is realized within the membrane and in the adjacent water layer, is crucial to achieve a specific assembly. In order to establish a well defined model system to study assembly processes in membranes, a recently reported D,Lalternating double helical hairpin construct in structural analogy to the natural antibiotic gramicidin A was utilized.[2,3] Recogntion at the membrane/water interface was addressed via met al complex formation as well as duplex formation of a short PNA sequence. To achieve recognition within the bilayer, nucleobases or polar amino acid residues, respectively, were introduced in the center of the hairpin TMD. Additionally, fluorophores were attached applying an orthogonal protecting group strategy. The functionalized TMDs were reconstituted in large unilamellar vesicles (LUVs). The in membrane pore formation by adopting 5.6 double helices was investigated using CD spectroscopy and the dynamic aggregation process was determined using fluorescence probes for Fluorescence Resonance Energy Transfer (FRET). For orientational studies as well as distance measurements of membrane incorporatedpeptide homodimer structures, spin probes were introduced within the lead structure. These homodimers were incorporated in LUVs and the 5.6 structure was determined via CD analysis. Further investigation will be performed applying EPR measurements. 172 pp. Englisch.

Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. KlappentextrnrnThe function of membrane proteins is mainly dependend on their aggregational behavior. Some are active as monomers, whereas others need to assemble into oligomeric states.1 In this context, molecular recognition, which is realized.

Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -The function of membrane proteins is mainly dependend on their aggregational behavior. Some are active as monomers, whereas others need to assemble into oligomeric states.1 In this context, molecular recognition, which is realized within the membrane and in the adjacent water layer, is crucial to achieve a specific assembly. In order to establish a well defined model system to study assembly processes in membranes, a recently reported D,Lalternating double helical hairpin construct in structural analogy to the natural antibiotic gramicidin A was utilized.[2,3] Recogntion at the membrane/water interface was addressed via met al complex formation as well as duplex formation of a short PNA sequence. To achieve recognition within the bilayer, nucleobases or polar amino acid residues, respectively, were introduced in the center of the hairpin TMD. Additionally, fluorophores were attached applying an orthogonal protecting group strategy. The functionalized TMDs were reconstituted in large unilamellar vesicles (LUVs). The in membrane pore formation by adopting 5.6 double helices was investigated using CD spectroscopy and the dynamic aggregation process was determined using fluorescence probes for Fluorescence Resonance Energy Transfer (FRET). For orientational studies as well as distance measurements of membrane incorporatedpeptide homodimer structures, spin probes were introduced within the lead structure. These homodimers were incorporated in LUVs and the 5.6 structure was determined via CD analysis. Further investigation will be performed applying EPR measurements.Cuvillier Verlag, Nonnenstieg 8, 37075 Göttingen 172 pp. Englisch.

Taschenbuch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - The function of membrane proteins is mainly dependend on their aggregational behavior. Some are active as monomers, whereas others need to assemble into oligomeric states.1 In this context, molecular recognition, which is realized within the membrane and in the adjacent water layer, is crucial to achieve a specific assembly. In order to establish a well defined model system to study assembly processes in membranes, a recently reported D,Lalternating double helical hairpin construct in structural analogy to the natural antibiotic gramicidin A was utilized.[2,3] Recogntion at the membrane/water interface was addressed via met al complex formation as well as duplex formation of a short PNA sequence. To achieve recognition within the bilayer, nucleobases or polar amino acid residues, respectively, were introduced in the center of the hairpin TMD. Additionally, fluorophores were attached applying an orthogonal protecting group strategy. The functionalized TMDs were reconstituted in large unilamellar vesicles (LUVs). The in membrane pore formation by adopting 5.6 double helices was investigated using CD spectroscopy and the dynamic aggregation process was determined using fluorescence probes for Fluorescence Resonance Energy Transfer (FRET). For orientational studies as well as distance measurements of membrane incorporatedpeptide homodimer structures, spin probes were introduced within the lead structure. These homodimers were incorporated in LUVs and the 5.6 structure was determined via CD analysis. Further investigation will be performed applying EPR measurements.

Taschenbuch. Condición: Neu. Synthesis and Aggregation of Peptidehelices in Artificial Membranes | Stefan Müllar | Taschenbuch | Englisch | 2012 | Cuvillier | EAN 9783954042869 | Verantwortliche Person für die EU: Cuvillier Verlag, Nonnenstieg 8, 37075 Göttingen, info[at]cuvillier[dot]de | Anbieter: preigu Print on Demand.