タシロ ミツル
田代 充 所属 理工学部 総合理工学科 職種 教授 |
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言語種別 | 英語 |
発行・発表の年月 | 2023 |
形態種別 | 学術雑誌 |
査読 | 査読あり |
標題 | Application of 31P NMR spectroscopy to analyze the affinity of 3’-AMP bound to proteins |
執筆形態 | 共著 |
掲載誌名 | Current Topics in Analytical Chemistry |
掲載区分 | 国外 |
出版社・発行元 | Research Trends |
巻・号・頁 | 14,pp.67-71 |
総ページ数 | 5 |
担当範囲 | NMR測定、執筆 |
担当区分 | 責任著者 |
著者・共著者 | K. Furihata, M. Tashiro |
概要 | Various 31P NMR techniques, including 31P-T1, 31P-T2, 31P-diffusion ordered spectroscopy and 31P{1H}saturation transfer difference techniques, were applied to analyze the affinity of adenosine 3’-monophosphate (3’-AMP) to human serum albumin. To date, no structures of the complex comprising 3’-AMP and human serum albumin have been deposited in Protein Data Bank. Because the 31P nucleus is a selective marker of phosphorylated compounds, its observation by NMR spectroscopy can be an effective method to investigate these molecular interactions in the solution state. In the present system, the 1H/31P-T2 measurements provided the sensitive results that confirmed complex formation, and simple comparisons of the 31P signal decay using the pulse sequence to measure 31P-T2 reflected these molecular interactions. The 31P{1H} saturation transfer difference experiment was also applied to confirm 3’-AMP bound to proteins. |