Determination of amino acid pairs in human p53 protein sensitive to mutations/variants by means of a random approach.
This is the continuation of our studies using random approaches to analyse the p53 protein family. In this data-based theoretical analysis, we use the random approach to analyse the amino acid pairs in human p53 protein in order to determine which amino acid pairs are more sensitive to 190 human p53 mutations/variants. The rationale of this study is based on our hypothesis and findings that a harmful mutation is more likely to occur at randomly unpredictable amino acid pairs, and a harmless mutation is more likely to occur at randomly predictable amino acid pairs. This is because we argue that the randomly predictable amino acid pairs should not be deliberately evolved, whereas the randomly unpredictable amino acid pairs should be deliberately evolved with a connection to protein function. The results show, for example, that 93.16% of 190 mutations/variants occur at randomly unpredictable amino acid pairs. Thus, the randomly unpredictable amino acid pairs are more sensitive to mutations/variants in human p53 protein. The results also suggest that the human p53 protein has a tendency for the occurrence of mutation/variants.
D000596:Amino Acids / Q000145:classification / Q000235:genetics*; D014644:Genetic Variation / Q000235:genetics; D006801:Humans; D008954:Models, Biological; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000235:genetics*
D000596:Amino Acids; D016159:Tumor Suppressor Protein p53