title: Molecular polarity in DNA-protein recognition--the case of lambda-repressor-operator system.
abstract: The charge distribution of lambda-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.
authors.forename: J H
authors.initials: JH
authors.lastname: Wang
authors.forename: M
authors.initials: M
authors.lastname: Lewis
mesh_terms: D010582:Bacteriophage lambda; D055592:Biophysical Phenomena; D001703:Biophysics; D004269:DNA, Bacterial; D004279:DNA, Viral; D004268:DNA-Binding Proteins / Q000502:physiology*; D012097:Repressor Proteins / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology*
chemical_list: D004269:DNA, Bacterial; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors