Abstract
The conformations of four β-amino acids in a model peptide environment were investigated using Hartree-Fock (HF) and density functional theory (DFT) methods in gas phase and with solvation. Initial structures were obtained by varying dihedral angles in increments of 45° in the range 0° - 360°. Stable geometries were optimized at both levels of theory with the correlation consistent double-zeta basis set with polarization functions (cc-pVDZ). The results suggest that solvation generally stabilizes the conformations relative to the gas phase and that intramolecular hydrogen bonding may play an important role in the stability of the conformations. The β3 structures, in which the R-group of the amino acid is located on the carbon atom next to the N-terminus, are somewhat more stable relative to each other than the β2 structures which have the R-group on the carbon next to the carbonyl.
Highlights
The functions of numerous biological systems depend on RNA and proteins
HF and density functional theory (DFT) were used to study the conformations of selected β-amino acids in both the gas phase and with solvation (DFT only)
The conformations of β-amino acids were investigated in the gas phase by HF and DFT calculations
Summary
Ngassa2*, Jie Song3 1School of Natural Sciences, Indiana University Southeast, New Albany, IN, USA 2Department of Chemistry, Grand Valley State University, Allendale, MI, USA 3Department of Chemistry and Biochemistry, University of Michigan-Flint, Flint, MI, USA
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