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Protein Domain Boundary Predictions: A Structural Biology Perspective

One of the important fields to apply computational tools for domain boundaries prediction is structural biology. They can be used to design protein constructs that must be expressed in a stable and functional form and must produce diffraction-quality crystals. However, prediction of protein domain b...

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Detalles Bibliográficos
Autores principales: Kirillova, Svetlana, Kumar, Suresh, Carugo, Oliviero
Formato: Texto
Lenguaje:English
Publicado: Bentham Open 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2669640/
https://www.ncbi.nlm.nih.gov/pubmed/19401756
http://dx.doi.org/10.2174/1874091X00903010001
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author Kirillova, Svetlana
Kumar, Suresh
Carugo, Oliviero
author_facet Kirillova, Svetlana
Kumar, Suresh
Carugo, Oliviero
author_sort Kirillova, Svetlana
collection PubMed
description One of the important fields to apply computational tools for domain boundaries prediction is structural biology. They can be used to design protein constructs that must be expressed in a stable and functional form and must produce diffraction-quality crystals. However, prediction of protein domain boundaries on the basis of amino acid sequences is still very problematical. In present study the performance of several computational approaches are compared. It is observed that the statistical significance of most of the predictions is rather poor. Nevertheless, when the right number of domains is correctly predicted, domain boundaries are predicted within very few residues from their real location. It can be concluded that prediction methods cannot be used yet as routine tools in structural biology, though some of them are rather promising.
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spelling pubmed-26696402009-04-28 Protein Domain Boundary Predictions: A Structural Biology Perspective Kirillova, Svetlana Kumar, Suresh Carugo, Oliviero Open Biochem J Article One of the important fields to apply computational tools for domain boundaries prediction is structural biology. They can be used to design protein constructs that must be expressed in a stable and functional form and must produce diffraction-quality crystals. However, prediction of protein domain boundaries on the basis of amino acid sequences is still very problematical. In present study the performance of several computational approaches are compared. It is observed that the statistical significance of most of the predictions is rather poor. Nevertheless, when the right number of domains is correctly predicted, domain boundaries are predicted within very few residues from their real location. It can be concluded that prediction methods cannot be used yet as routine tools in structural biology, though some of them are rather promising. Bentham Open 2009-01-21 /pmc/articles/PMC2669640/ /pubmed/19401756 http://dx.doi.org/10.2174/1874091X00903010001 Text en © Kirillova et al.; Licensee Bentham Open. http://creativecommons.org/licenses/by-nc/3.0/ This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
spellingShingle Article
Kirillova, Svetlana
Kumar, Suresh
Carugo, Oliviero
Protein Domain Boundary Predictions: A Structural Biology Perspective
title Protein Domain Boundary Predictions: A Structural Biology Perspective
title_full Protein Domain Boundary Predictions: A Structural Biology Perspective
title_fullStr Protein Domain Boundary Predictions: A Structural Biology Perspective
title_full_unstemmed Protein Domain Boundary Predictions: A Structural Biology Perspective
title_short Protein Domain Boundary Predictions: A Structural Biology Perspective
title_sort protein domain boundary predictions: a structural biology perspective
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2669640/
https://www.ncbi.nlm.nih.gov/pubmed/19401756
http://dx.doi.org/10.2174/1874091X00903010001
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