Analysis of amino acid pairs sensitive to variants in human collagen alpha5(IV) chain precursor by means of a random approach.
In this data-based theoretical analysis, we use the random approach to analyze the amino acid pairs in 5(IV) chain precursor (CA54) in order to determine which amino acid pairs are more sensitive to 151 variants from missense mutant human CA54 protein. The rationale of this study is based on our hypothesis and previous findings that harmful variance is more likely to occur at randomly unpredictable amino acid pair position rather than at randomly predictable positions. This is reasonable to argue as randomly predictable amino acid pairs are less likely to be deliberately evolved, whereas randomly unpredictable amino acid pairs are probably deliberately evolved in connection with protein function. The results show that all 151 variants occurred at randomly unpredictable amino acid pairs and the chance of a variant occurring is markedly higher in randomly unpredictable amino acid pairs than in predictable pairs. Thus, randomly unpredictable amino acid pairs are more sensitive to variance in human CA54. The results also suggest that the human CA54 protein has a natural tendency towards variants.
Wu
Guang
G
Laboratoire de Toxicocinétique et Pharmacocinétique, Faculté de Pharmacie, Université de la Méditerranée Aix-Marseille II, Marseille, France. hongguanglishibahao@yahoo.com
Yan
Shaomin
S
D000596:Amino Acids / Q000235:genetics* / Q000378:metabolism*; D003094:Collagen / Q000235:genetics* / Q000378:metabolism*; D019295:Computational Biology; D014644:Genetic Variation; D006801:Humans
D000596:Amino Acids; D003094:Collagen