NEXAFS study of glycine and glycine-based oligopeptides

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

doi:10.1016/j.elspec.2003.09.006

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

NEXAFS study of glycine and glycine-based oligopeptides

MPS-Authors

/persons/resource/persons211638

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

External Resource

https://www.sciencedirect.com/science/article/pii/S0368204803001701/pdfft?md5=7d34a7b7a67b309f0c3a856f5b4273f7&pid=1-s2.0-S0368204803001701-main.pdf
(全文テキスト（全般）)

https://doi.org/10.1016/j.elspec.2003.09.006
(全文テキスト（全般）)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

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.

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

要旨

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.