ISIS Neutron and Muon Source Data Journal

Copy of The effect of different ligands on the change in conformational entropy in BCA

Abstract: 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

Local Contact: Dr Mona Sarter
Experimenter: Dr Andreas Stadler

DOI: 10.5286/ISIS.E.RB2420502

ISIS Experiment Number: RB2420502

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Mona Sarter et al; (2025): Copy of The effect of different ligands on the change in conformational entropy in BCA, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB2420502

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