Abstract
Gene regulation requires transcription factors to efficiently recognize their target DNA site. Efficient recognition of target sequence is achieved by a facilitated diffusion process that combines 3D diffusion and 1D diffusive motions along the DNA, which are enabled by weak electrostatic (non-specific) interactions. The protein is presumed to scan the DNA while bound non-specifically, and lock into the specific binding site once it’s encountered. The mechanism by which a single domain protein alternates rapidly between these two binding modes is however unknown.
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