Studies on the Structure of Protein L7/L12 from Escherichia coli Ribosomes

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Abstract
Circular dichroism, infrared and proton magnetic resonance spectroscopy as well as microcalorimetry methods were used to investigate the intact proteins L7/L12 in solution and their different derivatives (L7 with oxidized residues of methionine, fragments 27–120, 1–73 and 74–120). On the basis of the data obtained the following conclusions have been drawn: (a) there is no β structure in the protein L7, (b) the N‐terminal region of L7 forms a long α helix, (c)the Phe‐30 residue within the N‐terminal region of L7 takes part in the dimerization, (d) the C‐terminal region of L7 is globular and (e) the Phe‐54 residue is included in the hydrophobic core of the globular C‐terminal region.