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Amino acid sequence of the cooperative homodimeric hemoglobin from the mollusc Scapharca inaequivalvis and topology of the intersubunit contacts
Author(s) -
Petruzzelli Raffaele,
Goffredo Bianca M.,
Barra Donatella,
Bossa Francesco,
Boffi Alberto,
Verzili Daniela,
Ascoli Franca,
Chiancone Emilia
Publication year - 1985
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(85)80632-3
Subject(s) - hemoglobin , myoglobin , sequence (biology) , topology (electrical circuits) , peptide sequence , chemistry , stereochemistry , amino acid , crystallography , biology , biochemistry , gene , combinatorics , mathematics
The dimeric hemoglobin (HbI) from Scapharca inaequivalvis is highly homologous to the other known dimeric Arcid hemoglobins. The sequence has a distinctive hydrophobicity profile in the region corresponding to the E and F helices with respect to both the hemoglobin and myoglobin chains from vertebrates due to the presence of several additional hydrophobic residues. The characteristic topology of the E and F helices is conserved in all the known sequences of Arcid hemoglobins including that of the so‐called α chain of the tetrameric component from Anadara trapezia . The rationale for this conservation lies in the unusual assembly of Arcid hemoglobins where the E and F helices are involved in the interdimeric contact. It is suggested that the extra hydrophobic residues play a major role in the assembly of the basic dimeric unit in these hemoglobins.