1. 13C=18O/15N isotope dependence of the amide-I/II 2D IR cross peaks for the fully extended peptides
- Author
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Maekawa, H, Ballano, G, Formaggio, F, Toniolo, C, and Ge, NH
- Subjects
Physical Chemistry ,Engineering ,Chemical Sciences ,Technology - Abstract
We have used a combination of 2D IR spectroscopy with 13C=18O labeled amide-I and 15N-labeled amide-II modes to reveal how vibrational coupling between labeled peptide units depends on secondary structure. Linear and 2D IR measurements and simulations of Cα,α-diethylglycine homotetrapeptide show that this compound adopts the fully extended (2.05-helical) conformation in CDCl3, consistent with previous work on the Ac-capped peptide. The amide-I/II cross peaks of isotopomers exhibit only a marginal isotope frequency shift between labeled modes that are separated by two peptide units, indicating a very weak coupling. This result is in sharp contrast with a large cross-peak shift observed in 310-helical peptides, in which the labeled amide-I and -II modes are connected through an inter-residue C=O···H-N hydrogen bond. The discovered 3D-structural dependence indicates that the 13C=18O/15N labeled amide-I/II cross peaks can distinguish the formation of a single 310-helical turn from the fully extended polypeptide chain and increase the versatility of 2D IR spectroscopy as a conformational analysis tool of biomolecules.
- Published
- 2014