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» Identifying Structural Motifs in Proteins
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BMCBI
2004
111views more  BMCBI 2004»
13 years 9 months ago
The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases
Background: The Hotdog fold was initially identified in the structure of Escherichia coli FabA and subsequently in 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. strain CB...
Shane C. Dillon, Alex Bateman
ISDA
2009
IEEE
14 years 4 months ago
MAHATMA: A Genetic Programming-Based Tool for Protein Classification
Proteins can be grouped into families according to some features such as hydrophobicity, composition or structure, aiming to establish common biological functions. This paper pres...
Denise Fukumi Tsunoda, Alex Alves Freitas, Heitor ...
BMCBI
2007
99views more  BMCBI 2007»
13 years 10 months ago
RepSeq - A database of amino acid repeats present in lower eukaryotic pathogens
Background: Amino acid repeat-containing proteins have a broad range of functions and their identification is of relevance to many experimental biologists. In human-infective prot...
Daniel P. Depledge, Ryan P. J. Lower, Deborah F. S...
BMCBI
2006
103views more  BMCBI 2006»
13 years 10 months ago
Cis-motifs upstream of the transcription and translation initiation sites are effectively revealed by their positional disequili
Background: The discovery of cis-regulatory motifs still remains a challenging task even though the number of sequenced genomes is constantly growing. Computational analyses using...
Kenneth W. Berendzen, Kurt Stüber, Klaus Hart...
RECOMB
2001
Springer
14 years 10 months ago
Predicting the beta-helix fold from protein sequence data
A method is presented that uses b-strand interactions to predict the parallel right-handed b-helix super-secondary structural motif in protein sequences. A program called BetaWrap...
Phil Bradley, Lenore Cowen, Matthew Menke, Jonatha...