The G surface protein of Paramecium primaurelia has important internal homologies and a periodic structure, which could be dictated in part by the rigid scaffolding of cysteine residues. The predicted secondary structure shows a quasi absence of α-helix and an abundance of β-pleated sheets and random coils. The monotony of the amino acid sequence is in favour of a structural role for the protein … expand

The G surface protein of Paramecium primaurelia has important internal homologies and a periodic structure, which could be dictated in part by the rigid scaffolding of cysteine residues. The predicted secondary structure shows a quasi absence of α-helix and an abundance of β-pleated sheets and random coils. The monotony of the amino acid sequence is in favour of a structural role for the protein [ PUBMED:3783679 ]. This structure is based on the presence of 37 periods of about 75 residues, each period containing eight cysteine residues [ PUBMED:2308165 ]. Homologies with other proteins are limited to surface antigens of trypanosomes.