Amino Acid Pairs Sensitive to Variants in Human Collagen alpha1(I) Chain Precursor

Abstract

In this data-based theoretical analysis, we use our random approach to analyse amino acid pairs in human collagen a 1(I) chain precursor (CA11) in order to determine which amino acid pairs are more sensitive to 95 variants with missense mutant in human CA11 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 that the randomly predictable amino acid pairs are less likely to be deliberately evolved, whereas the randomly unpredictable amino acid pairs are probably deliberately evolved in connection with protein function. The results show that all of 95 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 ones. Thus, the randomly unpredictable amino acid pairs are more sensitive to variance in human CA11 protein. Also the results suggest that the human CA11 protein has a natural tendency towards variants.