【摘 要】
：
Recent single molecule experiments have reported that DNA binding proteins (DNA-BPs) can diffuse along DNA [1].This suggests that interactions between proteins and DNA play a role during the target se
【机 构】
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University Pierre et Marie Curie France
【出 处】
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中国上海第七届国际新药发明科技年会
论文部分内容阅读
Recent single molecule experiments have reported that DNA binding proteins (DNA-BPs) can diffuse along DNA [1].This suggests that interactions between proteins and DNA play a role during the target search even far from their specific site on DNA.Here we show by means of Monte Carlo simulations and analytical calculations that there is a counterintuitive repulsion between the two oppositely charged macromolecules at a nanometer range.For the concave shape of DNA-BPs,and for realistic protein charge densities,we find that the DNA-protein interaction free energy has a minimum at a finite surface-to-surface separation,in which proteins can easily slide.When a protein encounters its target,the free energy barrier is completely counterbalanced by the H-bond interaction,thus enabling the sequence recognition [2].
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