| Atomic Force Microscope (AFM) has been developed to study the interaction of biologically interesting molecules. This study explores the possible application of AFM in the study of DNA-Protein interaction.;The first study investigated the interaction between the 3.4kb 5;AFM was used to image a 1.1kb fragment of Staphylococcus aureus HSP70 operon that contains a palindromic nucleotide sequence. Structural analysis of the fragment revealed a quadruplet that consists of a pair of stem-loops for which a novel 'SL2S' (Stem-Loop-Loop-Stem) model was proposed. AFM also revealed the binding of ORF37 to the quadruplet, establishing a molecular mechanism for this heat shock gene expression.;AFM was used to image entire human topoisomerase II a (p170). Molecular images obtained by AFM revealed homodimers exhibiting a "heart or donut-like" structure with a large axial pore.;AFM was used to investigate the action of the transcriptional repressor ATF3 on chopp10. AFM studies identified a ATF3 binding site, different from the Ap1 site and a C/EBP site that have been shown to be important in the repression of chopp10 gene expression by ATF3.;AFM was used to determine the smallest number of hexameric rings necessary to unwind DNA. A 1.13kb DNA fragment with 30 bases of non complimentary ssDNA tails on one end was used as a substrate to mimic replication fork. Analysis of images of 4A... |
