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Protein Engineering, Vol 10, 673-676, Copyright © 1997 by Oxford University Press


ARTICLES

Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method

M Cserzo, E Wallin, I Simon, G von Heijne and A Elofsson
Institute of Enzymology, Biological Research Center Hungarian Academy of Sciences, Budapest.

A new, simple method for predicting transmembrane segments in integral membrane proteins has been developed. It is based on low-stringency dot- plots of the query sequence against a collection of non-homologous membrane proteins using a previously derived scoring matrix [Cserzo et al., 1994, J. Mol. Biol., 243, 388-396]. This so-called dense alignment surface (DAS) method is shown to perform on par with earlier methods that require extra information in the form of multiple sequence alignments or the distribution of positively charged residues outside the transmembrane segments, and thus improves prediction abilities when only single-sequence information is available or for classes of membrane proteins that do not follow the 'positive inside' rule.
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