The polypeptide chains of collagen are composed of approximately 300 repeats of the amino-acid sequence, X-Y-Gly. X and Y can be any amino acids, but are most frequently proline (Pro) or 4(R)hydroxyproline (Hyp). These chains combine to form triple helices which are held together by strong H-bonds from the Gly N-H’s to the C=O’s of X and weak H-bonds from Pro C-H’s of Y to the C=O’s of X. We present geometric optimized triple helix calculations of Pro-Pro-Gly, Ala-Ala-Gly, azaGly-aza-Gly-Gly and Gly-Gly-Gly using B3LYP /D95(d,p) as the high and AM1 as the low levels in the ONIOM combine method in which the middle of six amino acid backbones are calculated at the high level (DFT), while the side chains and other six amino acids from N, C-terminal are calculated using the the low level (AM1). (Ala=Alanine, Gly=Glycine and azaGly=AzaGlycine)

Optimized collagen-like triple helix by density functional theory

2019 Spring National Meeting

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