Specific intermolecular interactions of conserved water molecules with amino acids in the Galectin-1 carbohydrate recognition domain

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 reveale...

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Detalles Bibliográficos
Autores principales: Di Lella, S., Petruk, A.A., De Armiño, D.J.A., Álvarez, R.M.S.
Formato: JOUR
Materias:
Binding energies
Galectin-1
Hydrogen-bonding interactions
Quantum chemical calculations
Amino acids
Binding energy
Bins
Carbohydrates
Chemical bonds
Crystal structure
Hydrogen bonds
Ligands
Methanol
Molecular biology
Molecular dynamics
Proteins
Quantum chemistry
Quantum theory
Bound water molecules
Carbohydrate-recognition domains
Hydrogen bonding interactions
Intermolecular interactions
Quantum mechanical method
Solvation properties
Biological functions
Molecules
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00222860_v978_n1-3_p220_DiLella
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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