NDLI: Thermodynamics Of Lectin-sugar Interaction: Binding Of Sugars To Winged Bean (Psophocarpus Tetragonolobus) Basic Agglutinin (WBAI)

Content Provider	Indian Institute of Science (IISc)
Author	Puri, Kamal Deep Surolia, Avadhesha
Copyright Year	1994
Abstract	Combining site of WBAI is extended and encompasses all the residues of blood group A-reactive trisaccharide [GalNAcalpha3Galbeta4Glc]. Though both of the fucose residues of A-pentasaccharide [GalNAcalpha(Fucalpha2)3Galbeta(Fucalpha3)4Glc] do not directly interact, with the combining site they thermodynamically favour the interaction of GalNAcalpha3Galbeta4Glc part of the molecule by imposing a sterically favourable orientation of the binding epitope viz. GalNAcalpha3Galbeta4Glc of the saccharide. Binding of sugars is driven by enthalpy and is devoid of heat capacity changes. This together with enthalpy-entropy compensation observed for these processes underscore the importance of water reorganization as being one of the principal determinant of protein-sugar interactions.
File Format	PDF
Journal	PeerReviewed
Language	English
Publisher	Pure and Applied Chemistry
Publisher Date	1994-01-01
Access Restriction	Authorized
Subject Keyword	Molecular Biophysics Unit
Content Type	Text
Resource Type	Article

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