The Relevance of Conformational Entropy for Protein-Ligand Interactions in Citrate Synthase
Molecular dynamics plays an important role for the biological function of enzymes. For protein ligand interactions, changes of conformational entropy of protein and hydration layer are relevant for the binding process. We suggest to investigate differences in protein dynamics and conformational entropy of citrate synthase (CS) in the ligand-free and in two different ligand-bound states by QENS on IN16B BATS mode. We would like to determine the change of conformational entropy Sconf of CS upon ligand binding from mean square displacements. Isothermal titration calorimetry (ITC) data will inform us about the entropy change S during ligand binding that includes both protein and hydration water components. By combining QENS and ITC results we will separate the contributions of protein Sconf and hydration water Shydr and how both of them regulate ligand binding in CS. We suggest to use the BATS mode to probe a large energy transfer range at high energy resolution for detailed line-shape analysis of the QENS broadening. Therefore, our experiment is not feasible on standard neutron backscattering spectrometers located at neutron reactors due to their restricted energy transfer range.
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Andreas M. Stadler; APPEL Markus; HARIS Luman and SEYDEL Tilo. (2021). The Relevance of Conformational Entropy for Protein-Ligand Interactions in Citrate Synthase. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-916
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