ISBN: 9783954042869

[ED: Taschenbuch], [PU: Cuvillier], Neuware - The function of membrane proteins is mainly dependend on their aggregational behavior. Some are active as monomers, whereas others need to as… Plus…

[ED: Taschenbuch], [PU: Cuvillier], 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.- Besorgungstitel - vorauss. Lieferzeit 3-5 Tage., DE, [SC: 2.40], Neuware, gewerbliches Angebot, 210x148x9 mm, 172, [GW: 231g], Banküberweisung, Offene Rechnung, Kreditkarte, PayPal, Offene Rechnung (Vorkasse vorbehalten), Internationaler Versand<

ISBN: 395404286X

[EAN: 9783954042869], Neubuch, [PU: Cuvillier], nach der Bestellung gedruckt Neuware - Printed after ordering - The function of membrane proteins is mainly dependend on their aggregationa… Plus…

[EAN: 9783954042869], Neubuch, [PU: Cuvillier], 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. 172 pp. Englisch, Books<

2012, ISBN: 9783954042869

Livres de poche

Cuvillier Verlag, Taschenbuch, Auflage: 1, 172 Seiten, Publiziert: 2012-11-29T00:00:01Z, Produktgruppe: Buch, 0.56 kg, Chemie, Naturwissenschaften & Technik, Kategorien, Bücher, Taschenbü… Plus…

Cuvillier Verlag, Taschenbuch, Auflage: 1, 172 Seiten, Publiziert: 2012-11-29T00:00:01Z, Produktgruppe: Buch, 0.56 kg, Chemie, Naturwissenschaften & Technik, Kategorien, Bücher, Taschenbücher, Fremdsprachige Bücher, Englische Bücher, Cuvillier Verlag, 2012<

ISBN: 395404286X

Synthesis and Aggregation of Peptidehelices in Artificial Membranes ab 29.74 € als Taschenbuch: 1. Aufl.. Aus dem Bereich: Bücher, Wissenschaft, Chemie, Medien > Bücher, Cuvillier

2012, ISBN: 395404286X

Kartoniert / Broschiert, mit Schutzumschlag 11, [PU:Cuvillier; Jentzsch-Cuvillier, Annette]