Random-coil chemical shifts of phosphorylated amino acids |
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Authors: | Ewa A Bienkiewicz Kevin J Lumb |
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Institution: | (1) Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, 80523-1870, U.S.A. |
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Abstract: | The 1H, 13C, 15N and 31 P random-coil chemical shifts and phosphate pKa values of the phosphorylated amino acids pSer, pThr and pTyr in the protected peptide Ac-Gly-Gly-X-Gly-Gly-NH2 have been obtained in water at 25 °C over the pH range 2 to 9. Analysis of ROESY spectra indicates that the peptides are unstructured. Phosphorylation induces changes in random-coil chemical shifts, some of which are comparable to those caused by secondary structure formation, and are therefore significant in structural analyses based on the chemical shift. |
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Keywords: | chemical shifts phosphorylation pKa values random coil |
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