Complete 1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein linkage region of serglycins.
We present complete 1H NMR assignments for two synthetic glycopeptides representative of the carbohydrate-protein linkage region of serglycin proteoglycans. The peptides are: Ser(Galp-Xylp)-Gly-Ser-Gly-Ser(Galp-Xylp)-Gly and, Ser(Galp-Xylp)-Gly-Ser(Galp-Xylp)-Gly-Ser(Galp-Xylp)-G ly. A number of 2D NMR spectra together with a 3D NOESY-TOCSY spectrum were acquired at 600 MHz to complete the assignments of the glycopeptides dissolved in water with 40% trifluoroethanol. Preliminary analysis of the NMR data suggests folded structures for the glycopeptides.
Curto
E V
EV
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham 35294-2041, USA.
Sakai
T T
TT
Jablonsky
M J
MJ
Rio-Anneheim
S
S
Jacquinet
J C
JC
Krishna
N R
NR
D002241:Carbohydrates / Q000737:chemistry*; D006020:Glycopeptides / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D011509:Proteoglycans / Q000737:chemistry*; D011522:Protons; D033921:Vesicular Transport Proteins
D002241:Carbohydrates; D006020:Glycopeptides; D011506:Proteins; D011509:Proteoglycans; D011522:Protons; D033921:Vesicular Transport Proteins; C075430:serglycin