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Symmetrical structure of the L7 protein dimer

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
178
Issue
1
Identifiers
DOI: 10.1016/0014-5793(84)81249-1
Keywords
  • Nmr Study
  • L7 Dimer Structure
  • L7 Monomer Structure
Disciplines
  • Biology

Abstract

Abstract 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.

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