ArticleNucleic acids research2008
Identifying foldable regions in protein sequence from the hydrophobic signal.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Molecular Properties of Globin Channels and Pores: Role of Cholesterol in Ligand Binding and Movement.Frontiers in physiology · 2016Article
- Protein inter-domain linker prediction using Random Forest and amino acid physiochemical properties.BMC bioinformatics · 2014Article
- Comprehensive repertoire of foldable regions within whole genomes.PLoS computational biology · 2013Article
- Article
- Comprehensively surveying structure and function of RING domains from Drosophila melanogaster.PloS one · 2011Article
- Article
- FIEFDom: a transparent domain boundary recognition system using a fuzzy mean operator.Nucleic acids research · 2009Article
- The Talpid3 gene (KIAA0586) encodes a centrosomal protein that is essential for primary cilia formation.Development (Cambridge, England) · 2009Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural genomics initiatives aim to elucidate representative 3D structures for the majority of protein families over the next decade, but many obstacles must be overcome. The correct design of constructs is extremely important since many proteins will be too large or contain unstructured regions and will not be amenable to crystallization. It is therefore essential to identify regions in protein sequences that are likely to be suitable for structural study. Scooby-Domain is a fast and simple method to identify globular domains in protein sequences. Domains are compact units of protein structure and their correct delineation will aid structural elucidation through a divide-and-conquer approach. Scooby-Domain predictions are based on the observed lengths and hydrophobicities of domains from proteins with known tertiary structure. The prediction method employs an A*-search to identify sequence regions that form a globular structure and those that are unstructured. On a test set of 173 proteins with consensus CATH and SCOP domain definitions, Scooby-Domain has a sensitivity of 50% and an accuracy of 29%, which is better than current state-of-the-art methods. The method does not rely on homology searches and, therefore, can identify previously unknown domains.
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Registered trials
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