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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
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author Yan, Shaomin
Wu, Guang
author_facet Yan, Shaomin
Wu, Guang
author_sort Yan, Shaomin
collection PubMed
description 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.
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spelling pubmed-70886322020-03-23 Mutation patterns in human α-galactosidase A Yan, Shaomin Wu, Guang Mol Divers Full-Length Paper 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. Springer Netherlands 2009-05-26 2010 /pmc/articles/PMC7088632/ /pubmed/19468850 http://dx.doi.org/10.1007/s11030-009-9158-4 Text en © Springer Science+Business Media B.V. 2009 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Full-Length Paper
Yan, Shaomin
Wu, Guang
Mutation patterns in human α-galactosidase A
title Mutation patterns in human α-galactosidase A
title_full Mutation patterns in human α-galactosidase A
title_fullStr Mutation patterns in human α-galactosidase A
title_full_unstemmed Mutation patterns in human α-galactosidase A
title_short Mutation patterns in human α-galactosidase A
title_sort mutation patterns in human α-galactosidase a
topic Full-Length Paper
url 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
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