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dc.creatorPapadopoulos, G.en
dc.creatorGrudinin, S.en
dc.creatorKalpaxis, D. L.en
dc.creatorCholi-Papadopoulou, T.en
dc.date.accessioned2015-11-23T10:43:11Z
dc.date.available2015-11-23T10:43:11Z
dc.date.issued2006
dc.identifier10.1007/s00249-006-0076-4
dc.identifier.issn0175-7571
dc.identifier.urihttp://hdl.handle.net/11615/31727
dc.description.abstractData from polyphenylalanine [poly(Phe)] synthesis determination in the presence and in the absence of erythromycin have been used in conjunction with Molecular Dynamics Simulation analysis, in order to localize the functional sites affected by mutations of Thermus thermophilus ribosomal protein L4 incorporated in Escherichia coli ribosomes. We observed that alterations in ribosome capability to synthesize poly(Phe) in the absence of erythromycin were mainly correlated to shifts of A2062 and C2612 of 23S rRNA, while in the presence of erythromycin they were correlated to shifts of A2060 and U2584 of 23S rRNA. Our results suggest a means of understanding the role of the extended loop of L4 ribosomal protein in ribosomal peptidyltransferase center.en
dc.sourceEuropean Biophysics Journal with Biophysics Lettersen
dc.source.uri<Go to ISI>://WOS:000240899300005
dc.subjectmolecular dynamicsen
dc.subjectribosomal functionen
dc.subjecterythromycinen
dc.subjectPEPTIDYL TRANSFERASE CENTERen
dc.subjectANGSTROM RESOLUTIONen
dc.subjectCRYSTAL-STRUCTUREen
dc.subjectRNAen
dc.subjectSUBUNITen
dc.subjectERYTHROMYCINen
dc.subjectANTIBIOTICSen
dc.subjectRESISTANCEen
dc.subjectTUNNELen
dc.subjectSITESen
dc.subjectBiophysicsen
dc.titleChanges in the level of poly(Phe) synthesis in Escherichia coli ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus can be explained by structural changes in the peptidyltransferase center: a molecular dynamics simulation analysisen
dc.typejournalArticleen


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