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Evaluation of transmembrane helix predictions in 2014.

Authors :
Reeb, Jonas
Kloppmann, Edda
Bernhofer, Michael
Rost, Burkhard
Source :
Proteins; Mar2015, Vol. 83 Issue 3, p473-484, 12p
Publication Year :
2015

Abstract

ABSTRACT Experimental structure determination continues to be challenging for membrane proteins. Computational prediction methods are therefore needed and widely used to supplement experimental data. Here, we re-examined the state of the art in transmembrane helix prediction based on a nonredundant dataset with 190 high-resolution structures. Analyzing 12 widely-used and well-known methods using a stringent performance measure, we largely confirmed the expected high level of performance. On the other hand, all methods performed worse for proteins that could not have been used for development. A few results stood out: First, all methods predicted proteins in eukaryotes better than those in bacteria. Second, methods worked less well for proteins with many transmembrane helices. Third, most methods correctly discriminated between soluble and transmembrane proteins. However, several older methods often mistook signal peptides for transmembrane helices. Some newer methods have overcome this shortcoming. In our hands, PolyPhobius and MEMSAT-SVM outperformed other methods. Proteins 2015; 83:473-484. © 2014 Wiley Periodicals, Inc. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
08873585
Volume :
83
Issue :
3
Database :
Complementary Index
Journal :
Proteins
Publication Type :
Academic Journal
Accession number :
100951356
Full Text :
https://doi.org/10.1002/prot.24749