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Current Topics in Analytical Chemistry   Volumes    Volume 14 
Application of 31P NMR spectroscopy to analyze the affinity of 3’-AMP bound to proteins
Kazuo Furihata, Mitsuru Tashiro
Pages: 67 - 71
Number of pages: 5
Current Topics in Analytical Chemistry
Volume 14 

Copyright © 2022 Research Trends. All rights reserved

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.
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