Charged forms of N-Formyl-L-histidinamide and ethylimidazole molecules were subjected to conformational analysis at the ab initio RHF/6-31G(d) level of theory. Side-chain potential energy surfaces, E = Ebb(X1,X2), were calculated at the nine typical backbone conformations (bb = αL, αD, βL, γL, γD, δL, δD, εL and εD) given by multidimensional conformational analysis (MDCA). Envisaged minima obtained from the topological analysis of E = Ebb(X1,X2) surfaces and from MDCA were fully optimized. Electrostatic interaction between charged side-chain and polar peptide bonds is discussed. Stabilization energy was calculated for each conformer of N-Formyl-L-histidinamide and scored relative to the stabilization energy of other amino acids.
- Ab initio
- Side-chain potential energy surface
ASJC Scopus subject areas
- Condensed Matter Physics
- Physical and Theoretical Chemistry