The influence of ligand binding on the dynamics of bovine carbonic anhydrase
Changes of protein conformational entropy ¿S_conf and hydration layers are relevant for ligand-binding. The protein-ligand binding is governed by equilibrium thermodynamics ¿G=¿H-T¿S, it occurs if ¿G is minimised. Previous work showed entropy-entropy compensation occurs between the protein streptavidin and its hydration layer. Another interesting system is bovine carbonic anhydrase II (BCAII). This protein has many compatible ligands. Two of these are 4-fluorobenzenesulfonamide (4-FBS) and pentafluorobenzenesulfonamide (PFBS). Analysing BCAII with 4-FBS and PFBS creates the opportunity to analyse different ligand binding affinities and their ¿S_conf. For this we aim to perform quasielastic neutron scattering experiments on BCAII in the ligand free and bound state for each ligand at different temperatures. We expect to see a negative ¿S_conf, as the ligand reduces the proteins flexibility
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The recommended format for citing this dataset in a research publication is in the following format:
SARTER Mona; HASSANI Abir Nesrine; SEYDEL Tilo and Andreas M. Stadler. (2023). The influence of ligand binding on the dynamics of bovine carbonic anhydrase. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-945
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This data is not yet public
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