| Title |
Protein-ligand binding volume determined from a single 2D NMR spectrum with increasing pressure / |
| Authors |
Skvarnavičius, Gediminas ; Toleikis, Zigmantas ; Michailovienė, Vilma ; Roumestand, Christian ; Matulis, Daumantas ; Petrauskas, Vytautas |
| DOI |
10.1021/acs.jpcb.1c02917 |
| Full Text |
|
| Is Part of |
The journal of physical chemistry. B.. Washington : American Chemical Society. 2021, vol. 125, iss. 22, p. 5823-5831.. ISSN 1520-6106. eISSN 1520-5207 |
| Keywords [eng] |
protein-ligand binding volume ; 2D NMR ; pressure |
| Abstract [eng] |
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. |
| Published |
Washington : American Chemical Society |
| Type |
Journal article |
| Language |
English |
| Publication date |
2021 |
| CC license |
|
