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From sequence:
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Disordered proteins:
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Protein solubility:
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Old 02-14-2017, 02:05 PM
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Default NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.

NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.

NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.

ACS Chem Biol. 2017 Feb 13;:

Authors: Gimeno A, Reichardt NC, Cañada FJ, Perkams L, Unverzagt C, Jimenez-Barbero J, Arda A

Abstract
Glycans play a key role as recognition elements in the communication of cells and other organisms. Thus, the analysis of carbohydrate-protein interactions has gained significant importance. In particular, Nuclear Magnetic Resonance (NMR) techniques are considered powerful tools to detect relevant features in the interaction between sugars and their natural receptors. Here we present the results obtained in the study on the molecular recognition of different mannose-containing glycans by Pisum Sativum Agglutinin. NMR experiments supported by Corcema-ST analysis, Isothermal Titration Calorimetry (ITC) experiments and Molecular Dynamics (MD) protocols have been successfully applied to unmask important binding features and especially to determine how a remote branching substituent significantly alters the binding mode of the sugar entity. These results highlight the key influence of common structural modifications in natural glycans on molecular recognition processes, and underscore their importance for the development of biomedical applications.


PMID: 28192664 [PubMed - as supplied by publisher]



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