Nuclear Overhauser Effect and Computational Characterization of the β-Spiral of the Polypentapeptide of Elastin

Abstract

The structure of the elastin polypentapeptide, poly(VPGVG), was studied by nuclear Overhauser effect experiments using perdeuterated Val¹ and Val⁴ samples under the condition where intermolecular interactions are absent. More extensive interaction was found between the Val¹ γCH and Pro² βCH protons than between the Val⁴ γCH and Pro² βCH protons. The Val¹ γCH₃—Pro² βCH interaction does not occur within the same pentamer as previously shown experimentally and as expected from steric considerations. The results are incompatible with the presence of a random chain network in poly(VPGVG) at room temperature but are readily explicable in terms of interturn interactions in a β-spiral structure. More specifically, the results indicate that the β-spiral conformation with 2.9 pentamers/turn is more prevalent than that with 2.7 pentamers/turn. Using conformations developed by molecular mechanics calculations, molecular dynamics simulations were carried out to compare the relative energies of these two variants of this class of β-spiral structures. It was found in vacuo that the structure with 2.9 pentamers/turn is indeed more stable than that of 2.7 pentamers/turn by ~ 1 kcal/mole-pentamer.