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Water‐protein and ligand‐protein interactions as determined by selective NMR relaxation studies
Author(s) -
Rossi Claudio,
Martini Silvia,
Ricci Maso,
Picchi Maria Pia,
Bonechi Claudia
Publication year - 2003
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.200351307
Subject(s) - macromolecule , ligand (biochemistry) , solvent , chemistry , relaxation (psychology) , nuclear magnetic resonance spectroscopy , computational chemistry , stereochemistry , organic chemistry , biochemistry , biology , receptor , neuroscience
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 ( R 1 SE ) and non‐selective ( R 1 NS ) 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 R 1 SE and ( R 1 NS ) analysis allowed the definition of the “affinity index”, [ A ] L T , an index related to the extent of the macromolecule‐ligand recognition process.