The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein.

@article{Gudkov1995TheF3,
  title={The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein.},
  author={Anatoly T. Gudkov and E V Budovskaya and N M Sherstobaeva},
  journal={FEBS letters},
  year={1995},
  volume={367 3},
  pages={280-2}
}
The ribosomal protein L7/L12 with the substitution of Cys38 for the Val38 residue was obtained and studied to test the orientation of polypeptide chains in the N-terminal region of the dimer. The results show that the L7/L12 dimer has a parallel (head-to-head) orientation of subunits and that its first 37 N-terminal residues are sufficient for dimerization.