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NEXAFS spectroscopy of homopolypeptides at all relevant absorption edges: polyisoleucine, polytyrosine, and polyhistidine

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

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Zubavichus, Y., Shaporenko, A., Grunze, M., & Zharnikov, M. (2007). NEXAFS spectroscopy of homopolypeptides at all relevant absorption edges: polyisoleucine, polytyrosine, and polyhistidine. The Journal of Physical Chemistry B, 111(33), 9803-9807. doi:10.1021/jp073922y.


Cite as: http://hdl.handle.net/21.11116/0000-0001-9C6F-4
Abstract
Carefully calibrated high-resolution low-noise near-edge X-ray absorption fine structure spectra of three homopolypetides, viz., polyisoleucine, polytyrosine, and polyhistidine at the C, N, and O K-edges, are compared with the respective spectra of parent amino acids and glycine-derived cyclic dipeptide, 2,5-diketopiperazine. An assignment of the spectral features related to the nitrogen and oxygen atoms constituting the peptide bond is suggested on the basis of a comparative analysis of the experimental spectra as well as theoretical calculations for 2,5-diketopiperazine within the real-space multiple-scattering formalism. A splitting of the pi*-feature in the N K-edge spectra is identified, which is probably sensitive to the dominant conformation type of the peptide molecule (i.e., alpha-helix vs beta-sheet).