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Symmetrical structure of the L7 protein dimer
Author(s) -
Bushuev V.N.,
Sepetov N.F.,
Gudkov A.T.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81249-1
Subject(s) - dimer , monomer , chemistry , sequence (biology) , amino acid residue , stereochemistry , protein structure , crystallography , peptide sequence , amino acid , biochemistry , organic chemistry , polymer , gene
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.