The ligand-macromolecule interaction is analysed in terms of selective (R1 SE) and non-selective (R1 NS) spin-lattice relaxation rates, considering the contribution arising from all possible specific and non-specific receptor sites. A linear relation between ΔR1 SE and macromolecule concentration is demonstrated to exist under any coordination conditions. The slope of the straight line obtained is defined as the 'affinity index' which is proposed as a general criterion for assessing the total ability of a ligand to interact with a macromolecule.

Rossi, C., Bastianoni, S., Bonechi, C., Corbini, G., Corti, P., Donati, A. (1999). Ligand-proteins recognition studies as determined by nuclear relaxation analysis. CHEMICAL PHYSICS LETTERS, 310(5-6), 495-500 [10.1016/S0009-2614(99)00811-8].

Ligand-proteins recognition studies as determined by nuclear relaxation analysis

ROSSI, CLAUDIO;BASTIANONI, SIMONE;BONECHI, CLAUDIA;CORBINI, GIANFRANCO;CORTI, PIERO;DONATI, ALESSANDRO
1999-01-01

Abstract

The ligand-macromolecule interaction is analysed in terms of selective (R1 SE) and non-selective (R1 NS) spin-lattice relaxation rates, considering the contribution arising from all possible specific and non-specific receptor sites. A linear relation between ΔR1 SE and macromolecule concentration is demonstrated to exist under any coordination conditions. The slope of the straight line obtained is defined as the 'affinity index' which is proposed as a general criterion for assessing the total ability of a ligand to interact with a macromolecule.
1999
Rossi, C., Bastianoni, S., Bonechi, C., Corbini, G., Corti, P., Donati, A. (1999). Ligand-proteins recognition studies as determined by nuclear relaxation analysis. CHEMICAL PHYSICS LETTERS, 310(5-6), 495-500 [10.1016/S0009-2614(99)00811-8].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/3641