Intramolecular carbohydrate-protein interaction.

J F Vliegenthart

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PubMed · 14533795

Intramolecular carbohydrate-protein interaction.

J F Vliegenthart

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Abstract

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.

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Amino Acid Sequence Binding Sites Bromelains Carbohydrate Sequence Carbohydrates Chorionic Gonadotropin Endoribonucleases Glycoproteins Glycosylation Humans In Vitro Techniques Molecular Sequence Data Molecular Structure Proteins Journal Article Research Support, Non-U.S. Gov't

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J F Vliegenthart. 2001. Intramolecular carbohydrate-protein interaction.. https://pubmed.ncbi.nlm.nih.gov/14533795/

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