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Updated: Oct 3, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Theoretical study for volume changes associated with the helix-coil transition of peptides
T Imai1, Y Harano, A Kovalenko
1Department of Theoretical Study, Institute for Molecular Science, Okazaki, 444-8585, Japan.
Abstract:
We calculate the partial molar volumes and their changes associated with the coil(extended)-to-helix transition of two types of peptide, glycine-oligomer and glutamic acid-oligomer, in aqueous solutions by using the Kirkwood-Buff solution theory coupled with the three-dimensional reference interaction site model (3D-RISM) theory. The volume changes associated with the transition are small and positive. The volume is analyzed by decomposing it into five contributions following the procedure proposed by Chalikian and Breslauer: the ideal volume, the van der Waals volume, the void volume, the thermal volume, and the interaction volume. The ideal volumes and the van der Waals volumes do not change appreciably upon the transition. In the both cases of glycine-peptide and glutamic acid-peptide, the changes in the void volumes are positive, while those in the thermal volumes are negative, and tend to balance those in the void volumes. The change in the interaction volume of glycine-peptide does not significantly contribute, while that of glutamic acid-peptide makes a negative contribution.
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