Structural features of Apramycin bound at the bacterial ribosome A site as detected by NMR and CD spectroscopy
Autor: | Balenci D., D'Amelio N., Gaggelli N., Cellai L., Molteni E., Valensin G. |
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Rok vydání: | 2010 |
Předmět: | |
Zdroj: | ChemBioChem 11 (2010): 166–169. info:cnr-pdr/source/autori:Balenci D., D'Amelio N., Gaggelli N., Cellai L., Molteni E., Valensin G./titolo:Structural features of Apramycin bound at the bacterial ribosome A site as detected by NMR and CD spectroscopy./doi:/rivista:ChemBioChem (Print)/anno:2010/pagina_da:166/pagina_a:169/intervallo_pagine:166–169/volume:11 |
Popis: | Transferred-NOE and CD techniques were found to provide a very convenient method for investigating the solution structure of kanamycin A interacting with a ribosomal A-site fragment. |
Databáze: | OpenAIRE |
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