INQUIMAE   12526
INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
artículos
Título:
Specific intermolecular interactions of conserved water molecules with amino acids in the Galectin-1 carbohydrate recognition domain
Autor/es:
DI LELLA, SANTIAGO; PETRUK, ARIEL ALCIDES; ALONSO DE ARMIÑO, DIEGO JAVIER; ÁLVAREZ, ROSA MARÍA SUSANA
Revista:
JOURNAL OF MOLECULAR STRUCTURE
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2010 vol. 978 p. 220 - 228
ISSN:
0022-2860
Resumen:
Water molecules, rigidly associated to protein surfaces, play a key
role in stabilizing biomolecules and participating in their biological
functions. Recent studies on the solvation properties of the
carbohydrate recognition domain of Galectin-1
by means of molecular dynamic simulations have revealed the existence
of several water sites which were well correlated to both the bound
water molecules observed in the crystal structure of the protein in the
free state and to some of the hydroxyl groups of the carbohydrate
ligand observed in the crystal structure of the complexed protein. In
this work, we present a study using quantum mechanical methods
(B3LYP/6-311++G(3df,3dp)//B3LYP/6-31+G(d)) to determine the energy
involved in the binding of these water molecules to specific amino
acids in the carbohydrate recognition domain of the protein. By
modeling the hydroxyl groups of the carbohydrate by methanol, the
energies associated to the local interactions between the ligand and
the protein have been evaluated by replacing specific water molecules
with methanol. The values of the binding energies have been compared to
those previously obtained by the molecular dynamic method.