Stop-flow fluorescence and photodiode array spectroscopy, with a millisecond time resolution, are used here to investigate refolding kinetics of the photoactive proton pump bacteriorhodopsin in mixed DMPC/CHAPS micelles from a partially denatured state in SDS. The study suggests that both the apoprotein folding and subsequent binding of retinal chromophore likely proceed via distinct multiple parallel pathways to generate the native helical bundle. Taken together, these data should have profound implications on the mechanisms of folding of proteins within biological membranes.
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Stop-flow fluorescence and photodiode array spectroscopy, with a millisecond time resolution, are used here to investigate refolding kinetics of the photoactive proton pump bacteriorhodopsin in mixed DMPC/CHAPS micelles from a partially denatured state in SDS. The study suggests that both the apoprotein folding and subsequent binding of retinal chromophore likely proceed via distinct multiple parallel pathways to generate the native helical bundle. Taken together, these data should have profound implications on the mechanisms of folding of proteins within biological membranes.
Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.
Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Stop-flow fluorescence and photodiode array spectroscopy, with a millisecond time resolution, are used here to investigate refolding kinetics of the photoactive proton pump bacteriorhodopsin in mixed DMPC/CHAPS micelles from a partially denatured state in SDS. The study suggests that both the apoprotein folding and subsequent binding of retinal chromophore likely proceed via distinct multiple parallel pathways to generate the native helical bundle. Taken together, these data should have profound implications on the mechanisms of folding of proteins within biological membranes. 152 pp. Englisch. N° de réf. du vendeur 9783838319438
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Vendeur : moluna, Greven, Allemagne
Etat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Stop-flow fluorescence and photodiode array spectroscopy, with a millisecond time resolution, are used here to investigate refolding kinetics of the photoactive proton pump bacteriorhodopsin in mixed DMPC/CHAPS micelles from a partially denatured state in S. N° de réf. du vendeur 5412615
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Vendeur : buchversandmimpf2000, Emtmannsberg, BAYE, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - Print on Demand Titel. Neuware -Stop-flow fluorescence and photodiode array spectroscopy, with a millisecond time resolution, are used here to investigate refolding kinetics of the photoactive proton pump bacteriorhodopsin in mixed DMPC/CHAPS micelles from a partially denatured state in SDS. The study suggests that both the apoprotein folding and subsequent binding of retinal chromophore likely proceed via distinct multiple parallel pathways to generate the native helical bundle. Taken together, these data should have profound implications on the mechanisms of folding of proteins within biological membranes.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 152 pp. Englisch. N° de réf. du vendeur 9783838319438
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Vendeur : AHA-BUCH GmbH, Einbeck, Allemagne
Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Stop-flow fluorescence and photodiode array spectroscopy, with a millisecond time resolution, are used here to investigate refolding kinetics of the photoactive proton pump bacteriorhodopsin in mixed DMPC/CHAPS micelles from a partially denatured state in SDS. The study suggests that both the apoprotein folding and subsequent binding of retinal chromophore likely proceed via distinct multiple parallel pathways to generate the native helical bundle. Taken together, these data should have profound implications on the mechanisms of folding of proteins within biological membranes. N° de réf. du vendeur 9783838319438
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Vendeur : preigu, Osnabrück, Allemagne
Taschenbuch. Etat : Neu. Folding Pathways of Photoactive Proton Pump Bacteriorhodopsin | A detailed kinetic study involving stop-flow spectroscopy to decipher the folding pathways of Bacteriorhodopsin | Amjad Farooq | Taschenbuch | 152 S. | Englisch | 2010 | LAP LAMBERT Academic Publishing | EAN 9783838319438 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. N° de réf. du vendeur 101292723
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