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which of the following statements concerning leucine zipper protein dimerization and dna binding is correct? A. Leucine zipper protein dimerization is facilitated by polar amino acids in the dimerization domains. B. Leucine zipper proteins contain many leucine amino acids in the DNA-binding region that facilitate sequence-specific DNA binding. C. Leucine zipper proteins function as a dimer with both subunits making contact with the sequence-specific DNA site. D. Leucine zipper proteins use ionic bonds to bind with the sequence-specific DNA site.

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The proper statement regarding leucine zipper protein dimerization and DNA binding is that polar amino acids in the dimerization domains assist leucine zipper protein dimerization. A vital biological process called protein dimerization occurs when proteins bind to produce functional assemblies, such as homo- or heterodimers.

The leucine zipper dimerization domain consists of four to five heptads, each of which has two -helical turns or seven amino acids, designated as amino acids a, b, c, d, e, f, and g. The leucine zipper oligomerization, dimerization stability, and dimerization selectivity are controlled by amino acids in the a, d, e, and g locations. The a and d locations of amino acids are often hydrophobic because they are on the same surface of the -helix.  Charged amino acids often reside in the g and e locations. The five C terminal amino acids in the g position interact with the oppositely charged amino acids in the e′ position in interhelical interactions, according to X-ray crystallography. Additionally, stability is aided by Van der Waal interactions between the underlying a and d amino acids and the g and e′ methylene groups.

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