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Prediction of genomic DNA mutation by DNA base pair polarity program
Author(s) -
Lee Suk Keun,
Kim Yeon Sook,
Lee Sang Shin,
Lee Young Joon,
Lee Yun Woo,
Park Sang Chul,
Chi Je Geun
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a658-a
Subject(s) - dna , base pair , biology , genomic dna , dna clamp , genetics , microbiology and biotechnology , gene , rna , reverse transcriptase
DNA double helix composed of pyrimidine and purine has important implications of genetic signals and machinery for DNA and RNA production, however, it showed antagonistic charge difference without electron transfer. Thus the distance between the pyrimidine and purine directly indicated the binding strength of DNA double helix affecting the DNA genetic cord conformation. Here, we made a DNA base pair polarity program using pyrimidine‐purine antagonism, of which hydrogen bond energy can be calculated. From the DNA base pair polarity the DNA segment could be outlined by the intramolecular electron circuit from pyrimidine group to purine group, and also the primary DNA section could be outlined by the electron transfer from negative DNA segment to adjacent 3′‐positive DNA segment. In the genomic DNA the distribution of DNA segment and section was different among the locus control region, promoter region, intron, and exon sequences. Here, we provide a new method to predict the heteropolymorphism, single nucleotide polymorphism, gene mutation in the genomic DNA. p53 gene mutation was widely investigated and turned out several critical changes in the phosphorylation site of p53 protein. Each of the mutation sites showed severe DNA base pair polarity, resulted in unbalanced DNA segments and sections greatly shifted into strong negativity of DNA hybridization energy level in the DNA codes. This presentation will show the DNA base pair polarity map of p53 gene including their DNA hybridization energy level, especially in the frequent mutation sites, i.e., P82, A143, H175, K317, K370, and K372.