NEXAFS study of glycine and glycine-based oligopeptides

Zubavichus, Y.; Zharnikov, M.; Schaporenko, A.; Grunze, Michael

doi:10.1016/j.elspec.2003.09.006

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NEXAFS study of glycine and glycine-based oligopeptides

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Grunze, Michael
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/S0368204803001701/pdfft?md5=7d34a7b7a67b309f0c3a856f5b4273f7&pid=1-s2.0-S0368204803001701-main.pdf
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Citation

Zubavichus, Y., Zharnikov, M., Schaporenko, A., & Grunze, M. (2004). NEXAFS study of glycine and glycine-based oligopeptides. Journal of Electron Spectroscopy and Related Phenomena, 134(1), 25-33. doi:10.1016/j.elspec.2003.09.006.

Cite as: https://hdl.handle.net/21.11116/0000-0001-D655-E

Abstract

Near-edge X-ray absorption fine structure (NEXAFS) spectra of glycine (Gly) and glycine-based oligopeptides, viz. diglycine (Digly), triglycine (Trigly), and 2,5-diketopiperazine, were measured at the C, N, and O K-edges in the partial electron yield mode. Differences between the spectra are discussed with their relation to electronic structures of the studied molecules. The emphasis is placed on spectral manifestations of the formation of the zwitter-ions and the building of peptide bonds.