Dynamics and Thermodynamics of Ligand–Protein Interactions

摘要: Protein–ligand interactions are of fundamental importance in a great many biological processes. However, despite enormous advances the speed and accuracy three-dimensional structure determination proteins their complexes, our ability to predict binding affinity from remains severely limited. One reason for this dilemma is that affinities governed not only by energetic considerations arising precise spatial disposition interacting groups (loosely, enthalpy), but also dynamics these entropy) including solvent effects. In work I will review current methodology unravelling complex problem, X-ray crystallography, NMR, isothermal titration calorimetry theoretical free energy perturbation methods.