{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,9]],"date-time":"2026-05-09T07:13:10Z","timestamp":1778310790821,"version":"3.51.4"},"reference-count":47,"publisher":"Oxford University Press (OUP)","issue":"13","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>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.<\/jats:p>\n               <jats:p>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 \u223c40% 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\u2013helix interface and (ii) sequence specificity as indicated by reduced affinity after mutating conserved residues.<\/jats:p>\n               <jats:p>Contact: \u00a0langosch@tum.de<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btt247","type":"journal-article","created":{"date-parts":[[2013,5,3]],"date-time":"2013-05-03T04:41:28Z","timestamp":1367556088000},"page":"1623-1630","source":"Crossref","is-referenced-by-count":16,"title":["Self-interaction of transmembrane helices representing pre-clusters from the human single-span membrane proteins"],"prefix":"10.1093","volume":"29","author":[{"given":"Jan","family":"Kirrbach","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miriam","family":"Krugliak","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian L.","family":"Ried","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Philipp","family":"Pagel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Isaiah T.","family":"Arkin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dieter","family":"Langosch","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2013,5,1]]},"reference":[{"key":"2023062614243606600_btt247-B1","doi-asserted-by":"crossref","first-page":"5362","DOI":"10.1021\/ja049826h","article-title":"Experimental measurement of the strength of a C alpha-H\u2026O bond in a lipid bilayer","volume":"126","author":"Arbely","year":"2004","journal-title":"J. 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