500 MHz NMR studies of the L7 monomer (oxidized protein) and of the dimer (intact protein) show that its N-terminal sequence takes part in the dimer formation. The identical environment of equivalent amino acid residues in different polypeptide chains in the dimer is evidence of the symmetrical structure of the L7 dimer. © 1984.
Bushuev, V. N., Sepetov, N. F., & Gudkov, A. T. (1984). Symmetrical structure of the L7 protein dimer. FEBS Letters, 178(1), 101–104. https://doi.org/10.1016/0014-5793(84)81249-1