Answer:
Assuming that the oligopeptide alphahelicks forms one continuous alpha-helix, the carbonyl oxygen of the glutamic acid residue is hydrogen bonded to the amide nitrogen of the next amino acid in the sequence.
In an alpha-helix, the peptide bonds between adjacent amino acids in the sequence are arranged in a spiral shape, with the carbonyl oxygen of one amino acid hydrogen bonded to the amide nitrogen of the next amino acid in the sequence. This arrangement helps to stabilize the alpha-helix and gives it its characteristic shape.
In the case of alphahelicks, the sequence of amino acids is Glu-Gly-Leu-Val-Lys-Lys-Glu, so the carbonyl oxygen of the glutamic acid (Glu) residue would be hydrogen bonded to the amide nitrogen of the glycine (Gly) residue. This is because the amide nitrogen of the glycine residue is the next amino acid in the sequence, and it is the amino acid that would be directly bonded to the carbonyl oxygen of the glutamic acid residue in the alpha-helix.