Hoffmann, R., Reichert, I., Wachs, W. O., Zeppezauer, M. and Kalbitzer, Hans Robert
(1994)
¹H and ³¹P NMR spectroscopy of phosphorylated model peptides.
International journal of peptide and protein research 44 (3), pp. 193-198.
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Abstract
The model peptides glycylglycyltyrosylalanine (Gly-Gly-Tyr-Ala), glycylglycylthreonylalanine (Gly-Gly-Thr-Ala) and glycylglycylserylalanine (Gly-Gly-Ser-Ala) were phosphorylated at the hydroxyl groups of their tyrosyl, threonyl and seryl residues, respectively, and characterized by 31P and 1H NMR spectroscopy. The pKa-value of the phosphoryl group in the tyrosine-containing peptide determined ...
Abstract
The model peptides glycylglycyltyrosylalanine (Gly-Gly-Tyr-Ala), glycylglycylthreonylalanine (Gly-Gly-Thr-Ala) and glycylglycylserylalanine (Gly-Gly-Ser-Ala) were phosphorylated at the hydroxyl groups of their tyrosyl, threonyl and seryl residues, respectively, and characterized by 31P and 1H NMR spectroscopy. The pKa-value of the phosphoryl group in the tyrosine-containing peptide determined from the pH dependence of chemical shifts is 5.9, the 31P chemical shifts at low pH (4.0) and high pH (8.0) are -3.8 and 0.2 ppm, respectively. Phosphorylation also leads to significant shifts of the 1H NMR resonances of the tyrosine residue; the amide resonance is shifted -0.02 ppm, the H alpha resonance 0.06 ppm, the H beta resonances 0.10 and -0.04 ppm, the H delta resonances 0.02 ppm and the H epsilon resonances 0.26 ppm. The pKa-value of the phosphoryl group in the threonine peptide determined from the pH dependence of chemical shifts is 6.1; the 31P chemical shifts at low pH (4.0) and high pH (8.0) are -0.1 and 4.8 ppm, respectively. The corresponding values for the serine peptide are 6.1 (pKa), 0.6 ppm and 4.9 ppm. Phosphorylation also leads to significant shifts of the 1H NMR resonances of the threonine and serine residues. In the threonine residue the amide resonance is shifted 0.25 ppm, the H alpha-resonance -0.43 ppm, the H beta-resonance 0.03 ppm and the H gamma-resonance 0.09 ppm. In the serine residue the amide resonance is shifted 0.21 ppm, the H alpha-resonance -0.17 ppm, and the H beta-resonances 0.17 ppm.
Export bibliographical data
| Item type: | Article |
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| Date: | 1994 |
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| Additional Information (public): | The journal of peptide research = online-Ausgabe |
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| Institutions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
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| Identification Number: | | Value | Type |
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| 7529751 | PubMed ID |
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| Classification: | | Notation | Type |
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| Amino Acid Sequence | MESH | | Hydrogen | MESH | | Kinetics | MESH | | Magnetic Resonance Spectroscopy/methods | MESH | | Molecular Sequence Data | MESH | | Oligopeptides/chemistry | MESH | | Phosphopeptides/chemistry | MESH | | Phosphorus | MESH | | Phosphoserine | MESH | | Phosphothreonine | MESH | | Phosphotyrosine | MESH | | Structure-Activity Relationship | MESH | | Tyrosine/analogs & derivatives | MESH |
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| Dewey Decimal Classification: | 500 Science > 570 Life sciences |
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| Status: | Published |
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| Refereed: | Unknown |
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| Created at the University of Regensburg: | Unknown |
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| Item ID: | 16499 |
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