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  1H and 31P NMR Spectroscopy of Phosphorylated Model Peptides

Hoffmann, R., Reichert, I., Wachs, W. O., Zeppezauer, M., & Kalbitzer, H. R. (1994). 1H and 31P NMR Spectroscopy of Phosphorylated Model Peptides. International journal of peptide and protein research, 44(3), 193-198. doi:10.1111/j.1399-3011.1994.tb00160.x.

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 Creators:
Hoffmann, Ralf, Author
Reichert, Ingmar, Author
Wachs, Wolfgang O., Author
Zeppezauer, Michael, Author
Kalbitzer, Hans Robert1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: phosphopeptide ; phosphothreonine ; phosphoserine ; phosphotyrosine ; 1H NMR ; 31P NMR ; random coil
 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.

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Language(s): eng - English
 Dates: 2009-01-121994-09-01
 Publication Status: Published in print
 Pages: 6
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 Table of Contents: -
 Rev. Type: Peer
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Title: International journal of peptide and protein research
  Abbreviation : Int. J. Pept. Prot. Res.
Source Genre: Journal
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Publ. Info: Copenhagen
Pages: - Volume / Issue: 44 (3) Sequence Number: - Start / End Page: 193 - 198 Identifier: ISSN: 0367-8377
ISSN: 0300-9769