Abstract
Conformational energy of the repeat pentapeptide of elastin, N-formyl-L-Val-L-Pro-Gly-L-Val-Gly-OCH3, was determined as a function of backbone torsion angles ϕ and ψ. Total conformational energy was assumed to consist of van der Waals, electrostatic, torsional, and hydrogen bond energies. Electrostatic energy was calculated using ab initio minimal basis set (STO-3G) net charges. Major conformational features observed are a ten-membered hydrogen-bonded type II β-turn system involving Val1 C'O and Val4 NH and a seven-membered equatorial (C7eq) conformation involving Gly3 C'O and Gly5 NH. The β-turn conformation is dominantly stabilized by the hydrogen-bond energy. A limited interaction is observed between Gly5 C'O and Gly3 NH. These theoretical results are compared with proton and carbon-13 magnetic resonance studies of this laboratory.
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