Inter-residue interactions in alpha-helical transmembrane proteins

Eduardo Mayol, Mercedes Campillo, Arnau Cordomí, Mireia Olivella

Research output: Contribution to journalArticleResearch

Abstract

© 2018 The Author(s) 2018. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com. Motivation: The number of available membrane protein structures has markedly increased in the last years and, in parallel, the reliability of the methods to detect transmembrane (TM) segments. In the present report, we characterized inter-residue interactions in α-helical membrane proteins using a dataset of 3462 TM helices from 430 proteins. This is by far the largest analysis published to date. Results: Our analysis of residue-residue interactions in TM segments of membrane proteins shows that almost all interactions involve aliphatic residues and Phe. There is lack of polar-polar, polar-charged and charged-charged interactions except for those between Thr or Ser sidechains and the backbone carbonyl of aliphatic and Phe residues. The results are discussed in the context of the preferences of amino acids to be in the protein core or exposed to the lipid bilayer and to occupy specific positions along the TM segment. Comparison to datasets of β-barrel membrane proteins and of α-helical globular proteins unveils the specific patterns of interactions and residue composition characteristic of α-helical membrane proteins that are the clue to understanding their structure. Availability and implementation: Results data and datasets used are available at http://lmc.uab.cat/TMalphaDB/interactions.php. Supplementary information: Supplementary data are available at Bioinformatics online.
Original languageEnglish
Pages (from-to)2578-2584
JournalBioinformatics
Volume35
DOIs
Publication statusPublished - 1 Aug 2019

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