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Molecular dynamics studies of mutations in p53

@ Atlanta University Center Robert W. Woodruff Library

Rohani, Leyla


ThesisM.S.PhysicsTumor protein p53 is a tumor suppressor that binds to a specific DNA sequence and trans-activates target genes leading to cell cycle arrest and/or apoptosis. p53, encoded by the human gene TP53, is a stress response protein that functions primarily as a tetrameric transcription factor, that regulates a large number of genes in response to a variety of cellular insults, including oncogene activation and DNA damage. Mutations in p53 are common in human cancer types. In order to study mutations in p53, 1TSR a wild type is selected along with four mutated proteins. The minimized conformation energy for the wild type and mutated proteins are calculated by simulated annealing using molecular dynamics simulations. The results show significant differences between hotspot mutations and the wild type in the minimized conformation energies using simulated annealing method. Based on the molecular dynamics, we have defined a correlation between molar masses of the target residue along with its two nearest neighbors to predict energy of a mutated protein respect to the wild type. Our results are in conformity with observations in the rate of mutation in biology.Electronic theses & dissertations collection for Atlanta University & Clark Atlanta University
Created Date:
2015 07 01
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DPLA: Include in Digital Public Library of America

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Atlanta University Center Robert W. Woodruff Library

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Digital Library of Georgia