New Insights into -GalNAc-Ser Motif: Influence of Hydrogen Bonding versus Solvent Interactions on the Preferred Conformation
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- 作者：Francisco Corzana ; Jesú ; s H. Busto ; Gonzalo Jimé ; nez-Osé ; s ; Juan L. Asensio ; Jesú ; s Jimé ; nez-Barbero ; Jesú ; s M. Peregrina ; Alberto Avenoza
- 刊名：Journal of the American Chemical Society
- 出版年：2006
- 出版时间：November 15, 2006
- 年：2006
- 卷：128
- 期：45
- 页码：14640 - 14648
- 全文大小：449K
- 年卷期：v.128,no.45(November 15, 2006)
- ISSN：1520-5126
文摘
The structural features of the mucin-type simplest model, namely, the glycopeptide 
-O-GalNAc-L-Ser diamide, have been investigated by combining NMR spectroscopy, molecular dynamics simulations,and DFT calculations. In contrast to previous reports, the study reveals that intramolecular hydrogen bondsbetween sugar and peptide residues are very weak and, as a consequence, not strong enough to maintainthe well-defined conformation of this type of molecule. In fact, the observed conformation of this modelglycopeptide can be satisfactorily explained by the presence of water pockets/bridges between the sugarand the peptide moieties. Additionally, DFT calculations reveal that not only the bridging water moleculesbut also the surrounding water molecules in the first hydration shell are essential to keep the existingconformation.
-O-GalNAc-L-Ser diamide, have been investigated by combining NMR spectroscopy, molecular dynamics simulations,and DFT calculations. In contrast to previous reports, the study reveals that intramolecular hydrogen bondsbetween sugar and peptide residues are very weak and, as a consequence, not strong enough to maintainthe well-defined conformation of this type of molecule. In fact, the observed conformation of this modelglycopeptide can be satisfactorily explained by the presence of water pockets/bridges between the sugarand the peptide moieties. Additionally, DFT calculations reveal that not only the bridging water moleculesbut also the surrounding water molecules in the first hydration shell are essential to keep the existingconformation.