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Owing to the strong hydrophilicity of their amino acid sequence and the nature of their secondary structure (beta strands), conventional hydropathy methods for predicting membrane topology are useless for this class of protein. The large number of available porin amino acid sequences was exploited to improve the accuracy of the prediction In combination with tools detecting amphipathicity of secondary structure. Using the constraints of \u03b2\u2010sheet structure these porins are predicted to contain 16 membrane\u2010spanning strands, 14 of which are common to the two (enteric and the neisserial) porin subfamilies.<\/jats:p>","DOI":"10.1111\/j.1365-2958.1991.tb02145.x","type":"journal-article","created":{"date-parts":[[2006,10,27]],"date-time":"2006-10-27T22:18:54Z","timestamp":1161987534000},"page":"2153-2164","source":"Crossref","is-referenced-by-count":225,"title":["The bacterial porin superfamily: sequence alignment and structure prediction"],"prefix":"10.1111","volume":"5","author":[{"given":"D.","family":"Jeanteur","sequence":"first","affiliation":[]},{"given":"J. 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