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A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method

Alpha-helical transmembrane protein (αTMP) is one of the two major categories of transmembrane protein (TMP). They are abundant existing in eukaryotic cells and involved in many biological processes. The special physicochemical properties, the structures of αTMP are hard to be experimentally solved,...

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Detalles Bibliográficos
Autores principales: Wang, Han, Wang, Jingru, Zhang, Li, Sun, Pingping, Du, Ning, Li, Yanwen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6036746/
https://www.ncbi.nlm.nih.gov/pubmed/29989071
http://dx.doi.org/10.7150/ijbs.24327
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author Wang, Han
Wang, Jingru
Zhang, Li
Sun, Pingping
Du, Ning
Li, Yanwen
author_facet Wang, Han
Wang, Jingru
Zhang, Li
Sun, Pingping
Du, Ning
Li, Yanwen
author_sort Wang, Han
collection PubMed
description Alpha-helical transmembrane protein (αTMP) is one of the two major categories of transmembrane protein (TMP). They are abundant existing in eukaryotic cells and involved in many biological processes. The special physicochemical properties, the structures of αTMP are hard to be experimentally solved, but αTMP's sequential segments are important to determine their conformations, so that TM-specific alignment is necessary to benefit their structure prediction. We used segment information extracted from topology structure and evolutionary information as features to implement a αTMP Segment Alignment method (TMSA). The method was trained using one non-redundant dataset and tested using another non-redundant dataset. Comparing the results to a general alignment method HHalign, TMSA achieved higher alignment accuracy, and easier to recognize the fold of αTMPs.
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spelling pubmed-60367462018-07-09 A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method Wang, Han Wang, Jingru Zhang, Li Sun, Pingping Du, Ning Li, Yanwen Int J Biol Sci Research Paper Alpha-helical transmembrane protein (αTMP) is one of the two major categories of transmembrane protein (TMP). They are abundant existing in eukaryotic cells and involved in many biological processes. The special physicochemical properties, the structures of αTMP are hard to be experimentally solved, but αTMP's sequential segments are important to determine their conformations, so that TM-specific alignment is necessary to benefit their structure prediction. We used segment information extracted from topology structure and evolutionary information as features to implement a αTMP Segment Alignment method (TMSA). The method was trained using one non-redundant dataset and tested using another non-redundant dataset. Comparing the results to a general alignment method HHalign, TMSA achieved higher alignment accuracy, and easier to recognize the fold of αTMPs. Ivyspring International Publisher 2018-05-22 /pmc/articles/PMC6036746/ /pubmed/29989071 http://dx.doi.org/10.7150/ijbs.24327 Text en © Ivyspring International Publisher This is an open access article distributed under the terms of the Creative Commons Attribution (CC BY-NC) license (https://creativecommons.org/licenses/by-nc/4.0/). See http://ivyspring.com/terms for full terms and conditions.
spellingShingle Research Paper
Wang, Han
Wang, Jingru
Zhang, Li
Sun, Pingping
Du, Ning
Li, Yanwen
A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method
title A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method
title_full A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method
title_fullStr A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method
title_full_unstemmed A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method
title_short A Sequential Segment Based Alpha-Helical Transmembrane Protein Alignment Method
title_sort sequential segment based alpha-helical transmembrane protein alignment method
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6036746/
https://www.ncbi.nlm.nih.gov/pubmed/29989071
http://dx.doi.org/10.7150/ijbs.24327
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