title: Mutation patterns in human alpha-galactosidase A.
abstract: A way to study the mutation pattern is to convert a 20-letter protein sequence into a scalar protein sequence, because the 20-letter protein sequence is neither vector nor scalar while a promising way to study patterns is in numerical domain. In this study, we use the amino-acid pair predictability to convert alpha-galactosidase A with its 137 mutations into scalar sequences, and analyse which amino-acid pairs are more sensitive to mutation. Our results show that the unpredictable amino-acid pairs are more sensitive to mutation, and the mutation trend is to narrow the difference between predicted and actual frequency of amino-acid pairs.
authors.affiliation: Guangxi Academy of Sciences, 98 Daling Road, Nanning, Guangxi Province, 530007, China.
authors.forename: Shaomin
authors.initials: S
authors.lastname: Yan
authors.forename: Guang
authors.initials: G
authors.lastname: Wu
mesh_terms: D000595:Amino Acid Sequence; D016009:Chi-Square Distribution; D019295:Computational Biology / Q000379:methods; D004252:DNA Mutational Analysis / Q000379:methods; D000795:Fabry Disease; D006801:Humans; D009154:Mutation; D020539:Sequence Analysis, Protein / Q000379:methods; D018709:Statistics, Nonparametric; D000519:alpha-Galactosidase / Q000737:chemistry / Q000235:genetics*
chemical_list: D000519:alpha-Galactosidase