Published August 1, 2004 | Version v1
Journal article

The effects of FEL irradiation against a phosphorylated peptide and the infrared spectrographic identification method for a phosphate group

Description

Phosphorylation and dephosphorylation, which are the most remarkable post-translational modifications, are considered to be important chemical reactions that control the activation of proteins. First, we examine the phosphorylation analysis method by measuring the infrared absorption peak of the phosphate group that is observed at about 1070 cm-1 (9.4 μm) with Fourier Transform-Infrared Spectrometer (FT-IR). Next, we attempt to control the quantity of phosphorylation, that is to say an action like dephosphorylation without enzyme reactions, by irradiating 9.4 μm-Free Electron Laser (9.4 μm-FEL). FEL irradiation has an effect of some kind on the organization of infrared absorption of a phosphate group. We would now like to go on to develop this photochemical reaction like dephosphorylation by examining under several conditions and in detail

Additional details

Identifiers

DOI
10.1016/j.nima.2004.04.113;
PII
S0168900204007892;

Publishing Information

Journal Title
Nuclear Instruments and Methods in Physics Research. Section A, Accelerators, Spectrometers, Detectors and Associated Equipment
Journal Volume
528
Journal Issue
1-2
Journal Page Range
p. 614-618
ISSN
0168-9002
CODEN
NIMAER

Conference

Title
25. international free electron laser conference; 10. FEL users workshop
Dates
8-12 Sep 2003
Place
Tsukuba, Ibaraki (Japan)

Optional Information

Copyright
Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.