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|Title:||Water-protein and ligand-protein interactions as determined by selective NMR relaxation studies||Authors:||Rossi, Claudio
Picchi, MARIA PIA
|Keywords:||Affinity index; NMR; relaxation; solvent-macromolecule interactions; water behaviour||Issue Date:||2003||Project:||None||Journal:||MACROMOLECULAR SYMPOSIA||Abstract:||
AbstractWater-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.
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