Random-coil chemical shifts of phosphorylated amino acids.
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.
Bienkiewicz
E A
EA
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins 80523-1870, USA.
Lumb
K J
KJ
D000596:Amino Acids / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000295:instrumentation / Q000379:methods*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry; D010759:Phosphorus Isotopes; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D012694:Serine / Q000737:chemistry; D013912:Threonine / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
D000596:Amino Acids; D010455:Peptides; D010759:Phosphorus Isotopes; D013912:Threonine; D014443:Tyrosine; D012694:Serine