Intramolecular carbohydrate-protein interaction.
In this report, an overview is presented of studies on the three-dimensional structure in solution of glycoproteins. The investigations were carried out by using high resolution NMR spectroscopy in conjunction with molecular dynamics calculations and molecular modelling. For pine apple stem bromelain, ribonuclease 2 and the free alpha-subunit of human chorionic gonadotropin it could be shown that intramolecular interactions between carbohydrate and protein exist. Glycosylation sites are rather unique structural entities in glycoproteins, because of the local spatial arrangements. This is reflected in different intramolecular interactions between carbohydrate and protein.
Vliegenthart
J F
JF
Bijvoet Center, Department Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands.
D000595:Amino Acid Sequence; D001665:Binding Sites; D001963:Bromelains / Q000737:chemistry; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000737:chemistry*; D006063:Chorionic Gonadotropin / Q000737:chemistry; D004722:Endoribonucleases / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry*
D002241:Carbohydrates; D006063:Chorionic Gonadotropin; D006023:Glycoproteins; D011506:Proteins; D001963:Bromelains; D004722:Endoribonucleases; C029494:ribonuclease U