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DNA–protein interaction is the reversible molecular association of a protein with DNA through noncovalent contacts that recognize nucleotide sequence, local DNA shape, helical geometry, chemical modifications, or higher-order nucleic-acid structures. The interaction is formed by combinations of electrostatic attraction between basic protein residues and the DNA phosphate backbone, hydrogen bonds, van der Waals contacts, water-mediated interactions, and contacts with exposed base edges in the major or minor groove ^[1][2]. DNA-binding proteins may engage DNA in sequence-selective or structure-selective binding modes and can recognize local conformational properties such as groove width, base-pair geometry, bending propensity, or single-stranded and noncanonical DNA structures ^[2][3]. Binding affinity, specificity, stoichiometry, cooperativity, residence time, and protein-induced conformational changes define the molecular properties of an individual DNA–protein complex ^[1][4]. Such interactions comprise the direct physical associations through which proteins access, organize, replicate, transcribe, repair, recombine, or package DNA ^[3][4].