Chiral discrimination and recognition is important in peptide biosynthesis, amino acid synthesis and drug designing. Detailed structural information is available about the peptide synthesis in ribosome. However, no detailed study is available about the discrimination in peptide synthesis. We study the conformational energy variation of neutral methoxy phenyl alanine molecule as a function of its different dihedral angle to locate the minimum energy conformation using quantum chemical theory. We compared the intermolecular energy surfaces of phenyl alanine molecule in its neutral and zwitterionic state using quantum chemical theory as a function of distance and mutual orientation. The energy surfaces are studied with rigid geometry by varying the distance and orientation. The potential energy surfaces of L-L and D-L pairs are found to be dissimilar and reflect the underlying chirality of the homochiral pair and racemic nature of the heterochiral pair. The intermolecular energy surface of homochiral pair is more favourable than the corresponding energy surface of heterochiral pair. © Indian Academy of Sciences.