Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3816
Title: Double-selective excitation techniques as a means of delineating dynamics of protein-bound small molecules
Authors: Marchettini, Nadia
Valensin, Gianni 
Issue Date: 1990
Project: None 
Journal: THE JOURNAL OF PHYSICAL CHEMISTRY
Abstract: 
A method for delineation of dynamics of protein-bound ligands is presented that relies on measuring 'H NMR spin-lattice relaxation rates upon double-selective excitation of dipolarly connected ligand resonances. Dipolar interaction energies of proton pairs are obtained in the free and bound states. For protons at fixed distances such dipolar energies are interpreted in terms of motional correlation times of relaxation vectors. As an example the reorientational correlation time of the indole moiety was evaluated at 23.5 ps for L-tryptophan in water solution and at 27.0 ns for L-tryptophan bound to human serum albumin.
Description: 
49496
URI: http://hdl.handle.net/20.500.12779/3816
ISSN: 0022-3654
DOI: 10.1021/j100374a030
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.