Assessing the conformation shift of transfer RNA phenylalanine in the presence of iron(II) and magnesium(II)
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The combining of the small subunit and large subunit (LSU) of the ribosome activates the synthesis and extension of a polypeptide through peptide bond formation at the peptidyl transferase center (PTC). This complex incorporates transfer RNA (tRNA) for the transfer of an amino acid to a growing polypeptide chain. Core sequences of ribosomal RNA (rRNA) are coordinated by magnesium cations and quasi-encapsulating ribosomal proteins. Superimposition of LSU crystal structures of many prokaryotic and archaeal species reveals a structurally conserved, magnesium rich core near the site of peptidyl transfer2. The structural change of tRNA in the presence of magnesium(II) could have serious implications for its interactivity with the PTC for peptidyl transfer. Circular dichroism spectroscopy was utilized to determine the structural change associated with the presence of magnesium(II).