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A tool for the prediction of functionally important sites in proteins using a library of functional templates.


ABSTRACT: UNLABELLED:Understanding and characterizing the biochemical and evolutionary information within the wealth of protein sequence and structural data, particularly at functionally important sites, is very important. A comprehensive analysis of physico-chemical properties and evolutionary conservation patterns at the molecular and biological function level is expected to yield important clues for identifying similar sites in as-yet uncharacterized proteins. We present a library of protein functional templates (PFTs) designed to represent the compositional and evolutionary conservation patterns of functional sites at the molecular and biological function level. Subsequently we developed LIMACS (LInear MAtching of Conservation Scores), a software tool that uses the template library for the prediction of functionally important sites in a multiple sequence alignment, transferring the molecular function annotation from the most-similar functional site in the template library to a predicted site. AVAILABILITY:The PFT library, the LIMACS program and source code are available for PC, Mac and Linux operating systems from ftp://ftp.ncbi.nih.gov/pub/lanczyck/limacs.

SUBMITTER: Lanczycki CJ 

PROVIDER: S-EPMC2374371 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature

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A tool for the prediction of functionally important sites in proteins using a library of functional templates.

Lanczycki Christopher J CJ   Chakrabarti Saikat S  

Bioinformation 20080222 7


<h4>Unlabelled</h4>Understanding and characterizing the biochemical and evolutionary information within the wealth of protein sequence and structural data, particularly at functionally important sites, is very important. A comprehensive analysis of physico-chemical properties and evolutionary conservation patterns at the molecular and biological function level is expected to yield important clues for identifying similar sites in as-yet uncharacterized proteins. We present a library of protein fu  ...[more]

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