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Theoretical conformational analysis of N-formyl-L-serine-L-alanine-NH2 dipeptide model was investigated using B3LYP/6-311+G(d,p) and M06-2X/6-311+G(d,p) calculations. In this research, 243 total possible conformations of the dipeptide model were optimized including 87 stable conformers and the other disappeared ones migrated to more stable geometries. Migration pattern suggests more stability of the dipeptide model with the serine (ser) in βL, γL, and γD and the alanine (ala) in γD and γL configurations, along with 26 of the found conf
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