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A novel mechanism is proposed for the AH/B interaction of sweet molecules, such as D-α-amino acids with the L-asparagine unit at the N-terminus of a receptor protein which has a right-handed α-helical conformation. The lipophilic, dispersive bonding occurs between the side chain of the fifth amino acid residue, from the N-terminus, and either the side chain of the α-amino acid or its methine group at the carbon 2. The sequence of AH, B and X groups on the sweet amino acids occurs in a clockwise orientation, when viewed from the receptor.
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Suami et al. (1991) studied this question.
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