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Mutation patterns in human α-galactosidase A

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...

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Detalles Bibliográficos
Autores principales: Yan, Shaomin, Wu, Guang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088632/
https://www.ncbi.nlm.nih.gov/pubmed/19468850
http://dx.doi.org/10.1007/s11030-009-9158-4
Descripción
Sumario: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 α-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.