Pressure Studies on Protein-Dna Interactions
作者： J. L. Silva , M. Villas-boas , R. M. Clegg
DOI: 10.1007/978-94-011-1699-2_27
关键词:
摘要: The use of hydrostatic pressure as a tool to study protein-DNA complexes is reported here for two systems: Arc repressor-DNA and nucleosomes. In the former case, it shown that magnitude stabilization subunit interaction was correlated with specificity interaction. Pressure-dissociation studies repressor in presence several synthetic DNAs same size (24 base pairs) were performed largest free energy association found operator DNA sequence. These results demonstrate importance free-energy linkage recognition process. second we examine high perturbation intact reconstituted nucleosome structure. single SH group H3 histones labeled specifically polar sensitive fluorophore acrylodan spectral shift emission fluorescence observed at different pressures ionic strengths. spectrum shifts red when applied, suggesting disassembly complex response application pressure, concomitant exposure solvent. This consistent major structural change closely juxtaposed 113 nucleosomal complex, exposing their contacting faces
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