Critical jump sizes in DNA-protein interactions
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Updated: Aug 2, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
1Department of Chemical Sciences, Tata Institute of Fundamental Research Homi Bhabha Road, Colaba, Mumbai, India, 400005. muruga@tifr.res.in
Abstract:
Interaction of a protein molecule with a specific-site on the DNA lattice can be modeled as an unbiased random jump process. Here we show that there exists a critical jump size (kc) beyond which site-specific association of a protein molecule with a DNA lattice cannot be facilitated. The maximum achievable association rate is predicted to be approximately 10(10) mol-1 s-1. This critical jump size scales with the total length of DNA lattice (N) as kc proportional, variantN2/3. Beyond kc the mean first passage time MFPT (denoted as T) required for the protein molecule to target the specific-site follows a linear scaling law as T proportional, variantN rather than the usual T proportional, variantN2 scaling law. On the basis of these results we argue that the evolution of the super coiled structures of the genomic DNA must be a consequence of the existence of this critical jump sizes. We finally show that the random jump method of searching for the specific-site by the protein molecule on the DNA lattice itself introduce an abstract linear type potential favoring the site-specific association rate.
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