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- W2113136627 abstract "Abstract Motivation: Most integral membrane proteins form dimeric or oligomeric complexes. Oligomerization is frequently supported by the non-covalent interaction of transmembrane helices. It is currently not clear how many high-affinity transmembrane domains (TMD) exist in a proteome and how specific their interactions are with respect to preferred contacting faces and their underlying residue motifs. Results: We first identify a threshold of 55% sequence similarity, which demarcates the border between meaningful alignments of TMDs and chance alignments. Clustering the human single-span membrane proteome using this threshold groups ∼40% of the TMDs. The homotypic interaction of the TMDs representing the 33 largest clusters was systematically investigated under standardized conditions. The results reveal a broad distribution of relative affinities. High relative affinity frequently coincides with (i) the existence of a preferred helix–helix interface and (ii) sequence specificity as indicated by reduced affinity after mutating conserved residues. Contact: langosch@tum.de Supplementary information: Supplementary data are available at Bioinformatics online." @default.
- W2113136627 created "2016-06-24" @default.
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- W2113136627 date "2013-05-01" @default.
- W2113136627 modified "2023-10-16" @default.
- W2113136627 title "Self-interaction of transmembrane helices representing pre-clusters from the human single-span membrane proteins" @default.
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- W2113136627 doi "https://doi.org/10.1093/bioinformatics/btt247" @default.
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