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Journal of Biomolecular NMR

, Volume 15, Issue 3, pp 203–206 | Cite as

Random-coil chemical shifts of phosphorylated amino acids

  • Ewa A. Bienkiewicz
  • Kevin J. Lumb
Article

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.

chemical shifts phosphorylation pKa values random coil 

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Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • Ewa A. Bienkiewicz
    • 1
  • Kevin J. Lumb
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyColorado State UniversityFort CollinsU.S.A.

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