Random-coil chemical shifts of phosphorylated amino acids

J Biomol NMR. 1999 Nov;15(3):203-6. doi: 10.1023/a:1008375029746.


The 1H, 13C, 15N and 31P random-coil chemical shifts and phosphate pKa values of 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 degrees 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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular / instrumentation
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Peptides / chemical synthesis
  • Peptides / chemistry
  • Phosphorus Isotopes
  • Phosphorylation
  • Protein Structure, Secondary
  • Serine / chemistry
  • Threonine / chemistry
  • Tyrosine / chemistry


  • Amino Acids
  • Peptides
  • Phosphorus Isotopes
  • Threonine
  • Tyrosine
  • Serine