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PMID: 9278280 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Protein engineering ·Vol. 10 ·No. 6 ·1997-06-00 ·Pages 673-6

Cserzö M, Wallin E, Simon I, von Heijne G, Elofsson A

Abstract

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 [Cserzö 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.

MeSH Terms
Cell Membrane/chemistry Computational Biology Membrane Proteins/analysis Models, Molecular Prokaryotic Cells/chemistry Protein Structure, Secondary Sequence Alignment/methods Sequence Homology, Amino Acid
Chemicals
Membrane Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Cserzö M
Institute of Enzymology, Biological Research Center Hungarian Academy of Sciences, Budapest.
Wallin E
Simon I
von Heijne G
Elofsson A
Article Info
Journal
Protein engineering
Abbr.
Protein Eng
ISSN
0269-2139
Published
1997-06-00
Pages
673-6
Language
English
Region
England
NLM ID
8801484
Subset
IM
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