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- W934128505 abstract "The first DNA-binding proteins studied by scientists were regulatory proteins from bacteria, where they act to control perhaps the simplest genetic systems found in nature. Today, the best characterized information about specific protein–DNA interactions in a living cell lies within the detailed structures of many different protein–DNA complexes, at near-atomic resolution. The specific interaction between 434 repressor protein and DNA seems to involve a sophisticated mixture of chemistry and three-dimensional geometry, which is known in general by the term “stereochemistry.” Many different amino acids must first fit together to make a large protein, which is perfectly complementary in its shape to the surface of the DNA formed by base pairs and phosphates, and then both surfaces must match closely so far as hydrogen bonds and hydrophobic contacts are concerned. Loss of just a few hydrogen bonds or hydrophobic contacts from an optimized protein–DNA complex will usually result in a large loss of specificity for the chosen DNA sequence, in comparison with others to which the protein might dock. Even before the protein and DNA come together, each “polar group” (for example, N–H, O–H, N, or O) will make hydrogen bonds to surrounding water molecules. Those hydrogen bonds to water will be mostly replaced in the protein–DNA complex by hydrogen bonds made directly between protein and DNA. It is essentially that concerted replacement of many different water molecules by protein or DNA, which causes the complex to become stable." @default.
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- W934128505 date "2004-01-01" @default.
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- W934128505 title "Specific DNA-Protein Interactions" @default.
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