FT-IR analysis of phosphorylated protein

Katsunori Ishii; Sachiko Suzuki Yoshihashi; Kunihiro Chihara; Kunio Awazu

doi:10.1117/12.541092

8 September 2004 FT-IR analysis of phosphorylated protein

Katsunori Ishii, Sachiko Suzuki Yoshihashi, Kunihiro Chihara, Kunio Awazu

Proceedings Volume 5461, Biophotonics New Frontier: From Genome to Proteome; (2004) https://doi.org/10.1117/12.541092
Event: Photonics Europe, 2004, Strasbourg, France

Abstract

Phosphorylation and dephosphorylation, which are the most remarkable posttranslational modifications, are considered to be important chemical reactions that control the activation of proteins. We examine the phosphorylation analysis method by measuring the infrared absorption peak of phosphate group that observed at about 1070cm^-1(9.4μm) with Fourier Transform Infrared Spectrometer (FT-IR). This study indicates that it is possible to identify a phosphorylation by measuring the infrared absorption peak of phosphate group observed at about 1070 cm^-1with FT-IR method. As long as target peptides have the same amino acid sequence, it is possible to identify the phosphorylated sites (threonine, serine and tyrosine).

Citation Download Citation

Katsunori Ishii, Sachiko Suzuki Yoshihashi, Kunihiro Chihara, and Kunio Awazu "FT-IR analysis of phosphorylated protein", Proc. SPIE 5461, Biophotonics New Frontier: From Genome to Proteome, (8 September 2004); https://doi.org/10.1117/12.541092

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