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CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
Circular permutation of a protein can be visualized as if the original amino- and carboxyl termini were linked and new ones created elsewhere. It has been well-documented that circular permutants usually retain native structures and biological functions. Here we report CPSARST (Circular Permutation...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2395249/ https://www.ncbi.nlm.nih.gov/pubmed/18201387 http://dx.doi.org/10.1186/gb-2008-9-1-r11 |
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author | Lo, Wei-Cheng Lyu, Ping-Chiang |
author_facet | Lo, Wei-Cheng Lyu, Ping-Chiang |
author_sort | Lo, Wei-Cheng |
collection | PubMed |
description | Circular permutation of a protein can be visualized as if the original amino- and carboxyl termini were linked and new ones created elsewhere. It has been well-documented that circular permutants usually retain native structures and biological functions. Here we report CPSARST (Circular Permutation Search Aided by Ramachandran Sequential Transformation) to be an efficient database search tool. In this post-genomics era, when the amount of protein structural data is increasing exponentially, it provides a new way to rapidly detect novel relationships among proteins. |
format | Text |
id | pubmed-2395249 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-23952492008-05-29 CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships Lo, Wei-Cheng Lyu, Ping-Chiang Genome Biol Method Circular permutation of a protein can be visualized as if the original amino- and carboxyl termini were linked and new ones created elsewhere. It has been well-documented that circular permutants usually retain native structures and biological functions. Here we report CPSARST (Circular Permutation Search Aided by Ramachandran Sequential Transformation) to be an efficient database search tool. In this post-genomics era, when the amount of protein structural data is increasing exponentially, it provides a new way to rapidly detect novel relationships among proteins. BioMed Central 2008-01-18 /pmc/articles/PMC2395249/ /pubmed/18201387 http://dx.doi.org/10.1186/gb-2008-9-1-r11 Text en Copyright © 2008 Lo et al.; licensee BioMed Central Ltd. https://creativecommons.org/licenses/by/2.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0 (https://creativecommons.org/licenses/by/2.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Method Lo, Wei-Cheng Lyu, Ping-Chiang CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships |
title | CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships |
title_full | CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships |
title_fullStr | CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships |
title_full_unstemmed | CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships |
title_short | CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships |
title_sort | cpsarst: an efficient circular permutation search tool applied to the detection of novel protein structural relationships |
topic | Method |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2395249/ https://www.ncbi.nlm.nih.gov/pubmed/18201387 http://dx.doi.org/10.1186/gb-2008-9-1-r11 |
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