Allostery is a physico-chemical phenomenon that regulates protein structure, flexibility and functions by signal transmission across nanometer distances within (or between) proteins. Allosteric signal transduction is ubiquitous in biological systems and regulates essential biochemical pathways. Understanding allostery at the atomistic level is crucial for controlling protein functions, providing roadmaps for the new developments in drug discovery and enzyme engineering. In this seminar, synergistic computational and experimental biophysical investigations [1-8] are illustrated, showing how important insights into allosteric mechanisms can be achieved for relevant biological systems, including a V-type allosteric enzyme [1-4, 7], a DNA-nuclear receptor complex  and the genoma-editing CRISPR-Cas9  and spliceosome  systems. In particular, community analysis of dynamical protein networks , see Figure 1, based on mutual information of correlated protein motions determined from classical molecular dynamics simulations will be described.
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