Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4785
Title: Water-protein and ligand-protein interactions as determined by selective NMR relaxation studies
Authors: Rossi, Claudio 
Martini, Silvia
Ricci, Maso
Picchi, MARIA PIA
Bonechi, Claudia 
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.
Description: 
49863
URI: http://hdl.handle.net/20.500.12779/4785
ISSN: 1022-1360
DOI: 10.1002/masy.200351307
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