Conformational preferences of N-acetyl-glyine-glycine-N'-methylamide: A theoretical study

Title
Conformational preferences of N-acetyl-glyine-glycine-N'-methylamide: A theoretical study
Authors
이호진박현미이강봉
Keywords
Ab initio; DFT; conformation; glycine; peptide
Issue Date
2009-10
Publisher
Journal of theoretical & computational chemistry
Citation
VOL 8, NO 5, 799-812
Abstract
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.
URI
http://pubs.kist.re.kr/handle/201004/36188
ISSN
0219-6336
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KIST Publication > Article
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