Conformational preferences of N-acetyl-glyine-glycine-N'-methylamide: A theoretical study
- Conformational preferences of N-acetyl-glyine-glycine-N'-methylamide: A theoretical study
- 이호진; 박현미; 이강봉
- Ab initio; DFT; conformation; glycine; peptide
- Issue Date
- Journal of theoretical & computational chemistry
- VOL 8, NO 5, 799-812
- The conformational preferences of peptide models have been investigated to understand the protein folding mechanism and to develop the force field. Here, we report the minimum energy conformations for a model peptide, N-acetyl–glycine–glycine–N′-methylamide (Ac–1Gly–2Gly–NHMe(I)) at the HF/3-21G, HF/6-31G*, and the B3LYP/6-31G* level of theory. At the B3LYP/6-31G* level, the 31 minima were identified and the 10 β-turn structures among the minima were observed in gas-phase. The conformational preferences of Gly residue in the model peptide, I depend on its relative position and conformation of neighboring Gly residue. The Gly residue in this model dipeptide has an asymmetric energy profile as one of Gly residue adopts a specific conformation. This study sheds some lights on understanding the unique conformational preferences of Gly residue in protein including two consecutive Gly residues.
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