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Default One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11

One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.

Related Articles One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.

J Protein Chem. 1990 Apr;9(2):129-36

Authors: Dill K, Hu SH, Berman E, Pavia AA, Lacombe JM

One- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy (at 11.7 Tesla) was used to gain some structural and spectral information about glycophorin AM, glycophorin AM tryptic glycopeptide, a related pentapeptide, and two related monoglycosylated pentapeptides. The protein spectral information suggests that the highly glycosylated N-terminus of glycophorin does not seem to possess a unique tertiary structure. Furthermore, the spectral information provided by the carbohydrate residues also indicates that there is no strong carbohydrate-protein interaction resulting in a unique tertiary structure. This result does not preclude any unique protein-carbohydrate interactions. For the small monoglycosylated pentapeptide containing alpha-D-GalNAc attached to Thr, a unique NOESY cross-peak was observed between the anomeric proton and the beta-proton of Thr. A cross-peak between the beta-proton of Ser and the anomeric proton was not observed for a related monoglycosylated pentapeptide containing alpha-D-GalNAc O-linked to Ser.

PMID: 2386609 [PubMed - indexed for MEDLINE]



Source: PubMed
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