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DOI: 10.3791/68674-v
Fabio C. L. Almeida1,2, Francisco Felipe Bezerra1,3, Ariana A. Vasconcelos1,2
1Institute of Medical Biochemistry Leopoldo de Meis (IBqM),Federal University of Rio de Janeiro (UFRJ), 2National Center for Structural Biology and Bioimaging (CENABIO),Federal University of Rio de Janeiro (UFRJ), 3Laboratory of Connective Tissue,Clementino Fraga Filho University Hospital
This NMR-based protocol investigates weak protein-glycan interactions using cyanovirin-N and D-mannose. Combining ligand- and protein-detected methods, it maps binding sites, detects allosteric effects, and identifies encounter complexes. The approach outlines sample preparation and data analysis, offering structural and dynamic insights valuable for glycan-specific diagnostics and recognition mechanisms.
We study protein-protein and protein-glycan interactions, focusing on integrin-disintegrin complex. Our model explores structural dynamics and highlight the role of surface force in mediating complex formation and interaction stability. Our group is dedicated to the study of the role of surface forces in molecular recognition and evolution of binding sites by studying surface hydrophobic clusters present in proteins.
NMR solution enables the detection of protein interactions. Although weak interactions are essential for life, there is a bias towards high-affinity complexes, even though they are present in many important biological functions. Our group is focusing on using integrative structural biology approaches to study large protein complex.
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