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Bridging protein local structures and protein functions

One of the major goals of molecular and evolutionary biology is to understand the functions of proteins by extracting functional information from protein sequences, structures and interactions. In this review, we summarize the repertoire of methods currently being applied and report recent progress...

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Detalles Bibliográficos
Autores principales: Liu, Zhi-Ping, Wu, Ling-Yun, Wang, Yong, Zhang, Xiang-Sun, Chen, Luonan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Vienna 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088341/
https://www.ncbi.nlm.nih.gov/pubmed/18421562
http://dx.doi.org/10.1007/s00726-008-0088-8
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author Liu, Zhi-Ping
Wu, Ling-Yun
Wang, Yong
Zhang, Xiang-Sun
Chen, Luonan
author_facet Liu, Zhi-Ping
Wu, Ling-Yun
Wang, Yong
Zhang, Xiang-Sun
Chen, Luonan
author_sort Liu, Zhi-Ping
collection PubMed
description One of the major goals of molecular and evolutionary biology is to understand the functions of proteins by extracting functional information from protein sequences, structures and interactions. In this review, we summarize the repertoire of methods currently being applied and report recent progress in the field of in silico annotation of protein function based on the accumulation of vast amounts of sequence and structure data. In particular, we emphasize the newly developed structure-based methods, which are able to identify locally structural motifs and reveal their relationship with protein functions. These methods include computational tools to identify the structural motifs and reveal the strong relationship between these pre-computed local structures and protein functions. We also discuss remaining problems and possible directions for this exciting and challenging area.
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spelling pubmed-70883412020-03-23 Bridging protein local structures and protein functions Liu, Zhi-Ping Wu, Ling-Yun Wang, Yong Zhang, Xiang-Sun Chen, Luonan Amino Acids Review Article One of the major goals of molecular and evolutionary biology is to understand the functions of proteins by extracting functional information from protein sequences, structures and interactions. In this review, we summarize the repertoire of methods currently being applied and report recent progress in the field of in silico annotation of protein function based on the accumulation of vast amounts of sequence and structure data. In particular, we emphasize the newly developed structure-based methods, which are able to identify locally structural motifs and reveal their relationship with protein functions. These methods include computational tools to identify the structural motifs and reveal the strong relationship between these pre-computed local structures and protein functions. We also discuss remaining problems and possible directions for this exciting and challenging area. Springer Vienna 2008-04-18 2008 /pmc/articles/PMC7088341/ /pubmed/18421562 http://dx.doi.org/10.1007/s00726-008-0088-8 Text en © Springer-Verlag 2008 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 Review Article
Liu, Zhi-Ping
Wu, Ling-Yun
Wang, Yong
Zhang, Xiang-Sun
Chen, Luonan
Bridging protein local structures and protein functions
title Bridging protein local structures and protein functions
title_full Bridging protein local structures and protein functions
title_fullStr Bridging protein local structures and protein functions
title_full_unstemmed Bridging protein local structures and protein functions
title_short Bridging protein local structures and protein functions
title_sort bridging protein local structures and protein functions
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088341/
https://www.ncbi.nlm.nih.gov/pubmed/18421562
http://dx.doi.org/10.1007/s00726-008-0088-8
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