Abstract
To investigate the short-range interactions in elastin, conformational energy calculations using ECEPP were carried out for elastin model tetrapeptide, Ac-Val-Pro-Gly-Gly-NHMe. The DCC* conformation is the most favorable one for Val-Pro-Gly portion in the model tetrapeptide. The bend in trans Ac-Val-Pro-Gly-Gly-NHMe are recognized at Pro-Gly and Gly-Gly portions with higher probability. Favorable bend type at Pro-Gly is type II and type V which is a distorted type II β-bend, and the summation of these bend probabilities is 0.60 which corresponds to the tendency of forming a type II β-bend at Pro-Gly supposed by experimental works in solution and crystal structure.
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Oka, M., Baba, Y., Kagemoto, A. et al. Theoretical Conformational Analysis on Elastin Model Tetrapeptide Ac-Val-Pro-Gly-Gly-NHMe. Polym J 21, 585–591 (1989). https://doi.org/10.1295/polymj.21.585
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DOI: https://doi.org/10.1295/polymj.21.585
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