eprintid: 24333
rev_number: 11
eprint_status: archive
userid: 1589
dir: disk0/00/02/43/33
datestamp: 2018-04-30 07:48:02
lastmod: 2024-03-11 07:51:59
status_changed: 2018-04-30 07:48:02
type: article
metadata_visibility: show
creators_name: Brüne, Daniel
creators_name: Navarro, Miguel A.
creators_name: Mier, Pablo
title: Proteome-wide comparison between the amino acid composition of domains and linkers
subjects: ddc-570
divisions: i-160100
abstract: Objective: Amino acid composition is a sequence feature that has been extensively used to characterize proteomes of many species and protein families. Yet the analysis of amino acid composition of protein domains and the linkers connecting them has received less attention. Here, we perform both a comprehensive full-proteome amino acid composition analysis and a similar analysis focusing on domains and linkers, to uncover domain- or linker-specific differential amino acid usage patterns.

Results: The amino acid composition in the 38 proteomes studied showcase the greater variability found in archaea and bacteria species compared to eukaryotes. When focusing on domains and linkers, we describe the preferential use of polar residues in linkers and hydrophobic residues in domains. To let any user perform this analysis on a given domain (or set of them), we developed a dedicated R script called RACCOON, which can be easily used and can provide interesting insights into the compositional differences between a domain and its surrounding linkers.
date: 2018
publisher: BioMed Central
id_scheme: DOI
ppn_swb: 1656060272
own_urn: urn:nbn:de:bsz:16-heidok-243339
language: eng
bibsort: BRUNEDANIEPROTEOMEWI2018
full_text_status: public
publication: BMC Research Notes
volume: 11
number: 117
place_of_pub: London
pagerange: 1-6
issn: 1756-0500
citation:   Brüne, Daniel ; Navarro, Miguel A. ; Mier, Pablo  (2018) Proteome-wide comparison between the amino acid composition of domains and linkers.  BMC Research Notes, 11 (117).  pp. 1-6.  ISSN 1756-0500     
document_url: https://archiv.ub.uni-heidelberg.de/volltextserver/24333/1/13104_2018_Article_3221.pdf