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- W2137342010 abstract "Analytical ultracentrifugation studies indicated that the C‐terminal domains of IF2 comprising amino acid residues 520–741 (IF2 C) and 632–741 (IF2 C‐2) bind fMet‐tRNA with similar affinities ( K d at 25°C equal to 0.27 and 0.23 μM, respectively). Complex formation between fMet‐tRNA fMet and IF2 C or IF2 C‐2 is accompanied by barely detectable spectral changes as demonstrated by a comparison of the Raman spectra of the complexes with the calculated sum of the spectra of the individual components. These results and the temperature dependence of the K d of the protein–RNA complexes indicate that complex formation is not accompanied by obvious conformational changes of the components, and possibly depends on a rather small binding site comprising only a few interacting residues of both components." @default.
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- W2137342010 date "2000-04-10" @default.
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- W2137342010 title "Interaction of fMet‐tRNA<sup>fMet</sup> with the C‐terminal domain of translational initiation factor IF2 from <i>Bacillus stearothermophilus</i>" @default.
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- W2137342010 doi "https://doi.org/10.1016/s0014-5793(00)01377-6" @default.
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