Protein-DNA interactions are fundamental in biology, evolution, disease, and biotechnology. This dissertation describes the use of state-of-the-art molecular modeling algorithms and supercomputing to more fully understand the molecular details of protein-DNA interfaces, anal to redesign protein-DNA recognition in order to create cutting edge reagents for genomic medicine. Here I show that all-atom physical modeling protocols derived from "first principles" and knowledge-based biophysical properties can recapitulate many native properties of DNA-binding proteins and enzymes, and can be used to rationally design the cleavage specificity of a homing endonuclease at multiple and adjacent base pairs.
|School:||University of Washington|
|School Location:||United States -- Washington|
|Source:||DAI-B 71/02, Dissertation Abstracts International|
|Keywords:||Gene therapy, Homing endonucleases, Protein-DNA interactions|
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