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Nuance in the double-helix and its role in protein-DNA recognition Rohs R; West SM; Liu P; Honig BCurr Opin Struct Biol 2009[Apr]; 19 (2): 171-7It has been known for some time that the double-helix is not a uniform structure but rather exhibits sequence-specific variations that, combined with base-specific intermolecular interactions, offer the possibility of numerous modes of protein-DNA recognition. All-atom simulations have revealed mechanistic insights into the structural and energetic basis of various recognition mechanisms for a number of protein-DNA complexes while coarser grained simulations have begun to provide an understanding of the function of larger assemblies. Molecular simulations have also been applied to the prediction of transcription factor binding sites, while empirical approaches have been developed to predict nucleosome positioning. Studies that combine and integrate experimental, statistical and computational data offer the promise of rapid advances in our understanding of protein-DNA recognition mechanisms.|*Nucleic Acid Conformation[MESH]|Binding Sites[MESH]|Computer Simulation[MESH]|DNA/*chemistry/metabolism[MESH]|Monte Carlo Method[MESH]|Nucleosomes/chemistry/metabolism[MESH]|Protein Conformation[MESH]|Proteins/*chemistry[MESH]|Transcription Factors/metabolism[MESH] |
