Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method.
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.
Cserzö
M
M
Institute of Enzymology, Biological Research Center Hungarian Academy of Sciences, Budapest.
Wallin
E
E
Simon
I
I
von Heijne
G
G
Elofsson
A
A
D002462:Cell Membrane / Q000737:chemistry; D019295:Computational Biology; D008565:Membrane Proteins / Q000032:analysis*; D008958:Models, Molecular; D011387:Prokaryotic Cells / Q000737:chemistry*; D017433:Protein Structure, Secondary; D016415:Sequence Alignment / Q000379:methods*; D017386:Sequence Homology, Amino Acid
D008565:Membrane Proteins