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In some cases [ 5, 6], the protein forms a dimer, and binds to the DNA in dimeric form.
In addition, GRK2 forms a dimer and binds Smo to stabilize its open conformation, and promote the dimerization of Smo C-tail.
Thus it forms a dimer made of quadruple hydrogen bonds.
The protein forms a dimer that straddles the cytoplasmic membrane.
Chromatography and SAXS suggest Dmd forms a dimer in solution consistent with that in crystal.
Compound 1 forms a dimer, compound 2 constitutes a chain and compound 3 forms a helix.
Importantly, the N-terminal Hera domain forms a dimer in the crystal similar to that seen in another thermophilic prokaryote.
The enzyme forms a dimer in the crystal structure with subunit orientations entirely different from the bacterial counterparts.
Arginine methyl ester forms a dimer; the dimer releases a heterocyclic compound and ornithine methyl ester at room temperature.
The chromodomain of Drosophila Polycomb (dPcCD) forms a dimer through the loop region connecting β4 and the C-terminal α-helix (Fig. 5B) (Min et al., 2003).
In all three forms of ATL, the molecule forms a dimer with the GTPase domains facing each other, but the position of the 3HB differs (Fig. 1B).
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