Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure.
J Phys Chem B
; 125(22): 5823-5831, 2021 06 10.
Article
in En
| MEDLINE
| ID: mdl-34032445
ABSTRACT
Proteins undergo changes in their partial volumes in numerous biological processes such as enzymatic catalysis, unfolding-refolding, and ligand binding. The change in the protein volume upon ligand binding-a parameter termed the protein-ligand binding volume-can be extensively studied by high-pressure NMR spectroscopy. In this study, we developed a method to determine the protein-ligand binding volume from a single two-dimensional (2D) 1H-15N heteronuclear single quantum coherence (HSQC) spectrum at different pressures, if the exchange between ligand-free and ligand-bound states of a protein is slow in the NMR time-scale. This approach required a significantly lower amount of protein and NMR time to determine the protein-ligand binding volume of two carbonic anhydrase isozymes upon binding their ligands. The proposed method can be used in other protein-ligand systems and expand the knowledge about protein volume changes upon small-molecule binding.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Magnetic Resonance Imaging
/
Proteins
Language:
En
Journal:
J Phys Chem B
Journal subject:
QUIMICA
Year:
2021
Document type:
Article
Affiliation country: