Conformational calculations of the N-terminal hydrophilic segment of human erythrocyte glycophorin.
The study is focused on the secondary structure of the external N-terminal segment of human erythrocyte glycophorin A (NN) which was determined by applying methods of CHOU et FASMAN and LIM. This hydrophilic glycophorin segment is assumed to consist of 48.5% ordered (alpha-helix, beta-sheet, beta-turn) and 51.5% unordered sequences. From the secondary structure suggestions are made concerning (i) peptide interaction and (ii) binding to the lipid bilayer of the N-terminal segment.
D000595:Amino Acid Sequence; D004912:Erythrocytes / Q000032:analysis*; D006021:Glycophorins; D006801:Humans; D011487:Protein Conformation; D012795:Sialoglycoproteins
D006021:Glycophorins; D012795:Sialoglycoproteins