Protein-DNA interaction the role of water as a facilitator

Fortunately, macromolecular crystallographic studies can now be used to explore the role of water in controlling both the specificity and the affinity of protein-DNA interactions [1 ]. Such analyses of protein-DNA crystal stmctures revealed that several distinct contributing factors are involved in such complex formation, such as HBs, 

The crystal structures of protein-DNA complexes reveal the presence of several ordered water molecules at protein-DNA interfaces. Such water molecules may reside in the solvation shells of the protein before their binding to DNA, and they may serve to fill all the gaps arising from imperfect matches of protein and DNA surfaces to maintain a suitable packing density for the system, or they may act as mediators of the protein-DNA recognition process. Some water molecules are also found in the interior cavities of such macromolecules. 

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Protein-DNA interaction the role of water as a facilitator References... 

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