Water‐protein and ligand‐protein interactions as determined by selective NMR relaxation studies | Zendy

Rossi Claudio | Zendy; Martini Silvia | Zendy; Ricci Maso | Zendy; Picchi Maria Pia | Zendy; Bonechi Claudia | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research