Intramolecular Hydrogen Bonding Motifs In Deprotonated Glycine Peptides Revealed By Cryogenic Ion Vibrational Spectroscopy

Duffy, Erin M.

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https://hdl.handle.net/2142/50864 Copy

Description

Title

Intramolecular Hydrogen Bonding Motifs In Deprotonated Glycine Peptides Revealed By Cryogenic Ion Vibrational Spectroscopy

Author(s)

Duffy, Erin M.

Contributor(s)

• Garand, Etienne
• Zhou, Jia
• Soukup, Michael
• Marsh, Brett

Issue Date

2014-06-17

Keyword(s)

Mini-symposium: Beyond the Mass-to-Charge Ratio: Spectroscopic Probes of the Structures of Ions

Abstract

We present the infrared spectra of deprotonated glycine chains, (\chem{Gly_n-H})$^{-}$, where n=1-4, obtained by cryogenic ion vibrational spectroscopy. Comparisons between the experimental and calculated spectra reveal the dependence on chain length of the hydrogen bonding motifs within these species. First, an interaction between the terminal carboxylate and the neighboring amide \chem{N-H} is present in all the peptide structures. In the longer (\chem{Gly_3-H})$^{-}$ and (\chem{Gly_4-H})$^{-}$ structures, the peptide chain folds such that the terminal \chem{NH_2} group also interacts with the carboxylate. Both of these also display an interaction between the terminal \chem{NH_2} and the neighboring amide \chem{N-H}. Finally, (\chem{Gly_4-H})$^{-}$ is the first among these species to contain an amide-amide interaction. Analysis of the \chem{N-H} peak positions elucidates the interplay among these different hydrogen bonds, especially around the negatively charged carboxylate moiety.

Publisher

International Symposium on Molecular Spectroscopy

Type of Resource

text

Language

English

Permalink

http://hdl.handle.net/2142/50864

DOI

https://doi.org/10.15278/isms.2014.TG12

Copyright and License Information

Copyright 2014 by the authors. Licensed under a Creative Commons Attribution 4.0 International License. http://creativecommons.org/licenses/by/4.0/

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