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Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures

BACKGROUND: Accurate and fast tools for comparing protein three-dimensional structures are necessary to scan and analyze large data sets. FINDINGS: The method described here is not only very fast but it is also reasonable precise, as it is shown by using the CATH database as a test set. Its rapidity...

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Detalles Bibliográficos
Autores principales: Kirillova, Svetlana, Carugo, Oliviero
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2535597/
https://www.ncbi.nlm.nih.gov/pubmed/18710497
http://dx.doi.org/10.1186/1756-0500-1-44
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author Kirillova, Svetlana
Carugo, Oliviero
author_facet Kirillova, Svetlana
Carugo, Oliviero
author_sort Kirillova, Svetlana
collection PubMed
description BACKGROUND: Accurate and fast tools for comparing protein three-dimensional structures are necessary to scan and analyze large data sets. FINDINGS: The method described here is not only very fast but it is also reasonable precise, as it is shown by using the CATH database as a test set. Its rapidity depends on the fact that the protein structure is represented by vectors that monitors the distribution of the inter-residue distances within the protein core and the structure of which is optimized with the Freedman-Diaconis rule. CONCLUSION: The similarity score is based on a χ(2 )test, the probability density function of which can be accurately estimated.
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spelling pubmed-25355972008-09-15 Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures Kirillova, Svetlana Carugo, Oliviero BMC Res Notes Project Note BACKGROUND: Accurate and fast tools for comparing protein three-dimensional structures are necessary to scan and analyze large data sets. FINDINGS: The method described here is not only very fast but it is also reasonable precise, as it is shown by using the CATH database as a test set. Its rapidity depends on the fact that the protein structure is represented by vectors that monitors the distribution of the inter-residue distances within the protein core and the structure of which is optimized with the Freedman-Diaconis rule. CONCLUSION: The similarity score is based on a χ(2 )test, the probability density function of which can be accurately estimated. BioMed Central 2008-07-11 /pmc/articles/PMC2535597/ /pubmed/18710497 http://dx.doi.org/10.1186/1756-0500-1-44 Text en Copyright © 2008 Kirillova and Carugo; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Project Note
Kirillova, Svetlana
Carugo, Oliviero
Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures
title Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures
title_full Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures
title_fullStr Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures
title_full_unstemmed Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures
title_short Progress in the PRIDE technique for rapidly comparing protein three-dimensional structures
title_sort progress in the pride technique for rapidly comparing protein three-dimensional structures
topic Project Note
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2535597/
https://www.ncbi.nlm.nih.gov/pubmed/18710497
http://dx.doi.org/10.1186/1756-0500-1-44
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