Abstract Water-macromolecules and ligand-macromolecules interactions were investigated considering the effects induced by the presence of a macromolecule on both the water and the ligand NMR selective (R1SE) and non-selective (R1NS) spin-lattice relaxation rates. The results obtained from the solvent studies were used to describe the solvent dynamics at the macromolecule-solvent interface. On the other hand, ligand R1SE and (R1NS) analysis allowed the definition of the “affinity index”, [A]LT, an index related to the extent of the macromolecule-ligand recognition process.

Rossi, C., Martini, S., Ricci, M., Picchi, M.P., Bonechi, C. (2003). Water-protein and ligand-protein interactions as determined by selective NMR relaxation studies. MACROMOLECULAR SYMPOSIA, 203, 89-102 [10.1002/masy.200351307].

Water-protein and ligand-protein interactions as determined by selective NMR relaxation studies

ROSSI, CLAUDIO;MARTINI, SILVIA;RICCI, MASO;PICCHI, MARIA PIA;BONECHI, CLAUDIA
2003-01-01

Abstract

Abstract Water-macromolecules and ligand-macromolecules interactions were investigated considering the effects induced by the presence of a macromolecule on both the water and the ligand NMR selective (R1SE) and non-selective (R1NS) spin-lattice relaxation rates. The results obtained from the solvent studies were used to describe the solvent dynamics at the macromolecule-solvent interface. On the other hand, ligand R1SE and (R1NS) analysis allowed the definition of the “affinity index”, [A]LT, an index related to the extent of the macromolecule-ligand recognition process.
Rossi, C., Martini, S., Ricci, M., Picchi, M.P., Bonechi, C. (2003). Water-protein and ligand-protein interactions as determined by selective NMR relaxation studies. MACROMOLECULAR SYMPOSIA, 203, 89-102 [10.1002/masy.200351307].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/34258
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