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@ARTICLE{Papadopoulos:56130,
      author       = {Papadopoulos, G. and Grudinin, S. and Kalpaxis, D. and
                      Choli-Papadopoulou, T.},
      title        = {{C}hanges in the level of poly({P}he) synthesis in
                      {E}scherichia coli ribosomes containing mutants of {L}4
                      ribosomal protein from {T}hermus thermophilus can be
                      explained by structural changes in the peptidyltransferase
                      center: a molecular dynamics simulation anal.},
      journal      = {European biophysics journal},
      volume       = {35},
      issn         = {0175-7571},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PreJuSER-56130},
      pages        = {675 - 683},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Data 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.},
      keywords     = {Amino Acid Sequence / Anti-Bacterial Agents: pharmacology /
                      Erythromycin: pharmacology / Escherichia coli: drug effects
                      / Escherichia coli: genetics / Escherichia coli: metabolism
                      / Models, Molecular / Molecular Sequence Data / Mutation /
                      Nucleic Acid Conformation / Peptides: metabolism / Peptidyl
                      Transferases: chemistry / Peptidyl Transferases: metabolism
                      / Protein Conformation / RNA, Bacterial: genetics / RNA,
                      Ribosomal, 23S: genetics / Ribosomal Proteins: chemistry /
                      Ribosomal Proteins: genetics / Ribosomal Proteins:
                      metabolism / Ribosomes: genetics / Ribosomes: metabolism /
                      Thermus thermophilus: metabolism / Anti-Bacterial Agents
                      (NLM Chemicals) / Peptides (NLM Chemicals) / RNA, Bacterial
                      (NLM Chemicals) / RNA, Ribosomal, 23S (NLM Chemicals) /
                      Ribosomal Proteins (NLM Chemicals) / ribosomal protein L4
                      (NLM Chemicals) / Erythromycin (NLM Chemicals) /
                      polyphenylalanine (NLM Chemicals) / Peptidyl Transferases
                      (NLM Chemicals) / J (WoSType)},
      cin          = {IFF-TH-II},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB31},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16773394},
      UT           = {WOS:000240899300005},
      doi          = {10.1007/s00249-006-0076-4},
      url          = {https://juser.fz-juelich.de/record/56130},
}