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The charge distribution of λ-repressor suggests that the molecular electrostatic polarity may accelerate the non-specific binding of the protein to the DNA molecule. The repressor molecule has a patch of positive charge within the first 26 residues which may contribute a non-specific binding surface. In addition, electrostatics may play an important role and account for why proteins form and use dimers in many specific DNA-protein recognition processes.
The charge distribution of λ-repressor suggests that the molecular electrostatic polarity may accelerate the non-specific binding of the protein to the DNA molecule. The repressor molecule has a patch of positive charge within the first 26 residues which may contribute a non-specific binding In addition, electrostatics may play an important role and account for why proteins form and use dimers in many specific DNA-protein recognition processes.