A simple statistical method for discriminating outer membrane proteins with better accuracy
Open Access
- 5 November 2004
- journal article
- research article
- Published by Oxford University Press (OUP) in Bioinformatics
- Vol. 21 (7) , 961-968
- https://doi.org/10.1093/bioinformatics/bti126
Abstract
Motivation: Discriminating outer membrane proteins from other folding types of globular and membrane proteins is an important task both for identifying outer membrane proteins from genomic sequences and for the successful prediction of their secondary and tertiary structures. Results: We have systematically analyzed the amino acid composition of globular proteins from different structural classes and outer membrane proteins. We found that the residues, Glu, His, Ile, Cys, Gln, Asn and Ser, show a significant difference between globular and outer membrane proteins. Based on this information, we have devised a statistical method for discriminating outer membrane proteins from other globular and membrane proteins. Our approach correctly picked up the outer membrane proteins with an accuracy of 89% for the training set of 337 proteins. On the other hand, our method has correctly excluded the globular proteins at an accuracy of 79% in a non-redundant dataset of 674 proteins. Furthermore, the present method is able to correctly exclude α-helical membrane proteins up to an accuracy of 80%. These accuracy levels are comparable to other methods in the literature, and this is a simple method, which could be used for dissecting outer membrane proteins from genomic sequences. The influence of protein size, structural class and specific residues for discrimination is discussed. Availability: A program for the discrimination method is available upon request from the corresponding author. The datasets used in this work are available at http://www.cbrc.jp/~gromiha/omp/dataset.html Contact:michael-gromiha@aist.go.jpKeywords
This publication has 46 references indexed in Scilit:
- Neural network‐based prediction of transmembrane β‐strand segments in outer membrane proteinsJournal of Computational Chemistry, 2004
- Identification of β-barrel membrane proteins based on amino acid composition properties and predicted secondary structureComputational Biology and Chemistry, 2003
- Profiles from structure based sequence alignment of porins can identify β stranded integral membrane proteinsBioinformatics, 2000
- High-resolution structure of the OmpA membrane domainJournal of Molecular Biology, 2000
- The Protein Data BankNucleic Acids Research, 2000
- A simple method for predicting transmembrane α helices with better accuracyProtein Engineering, Design and Selection, 1999
- Prediction of transmembrane β‐strands from hydrophobic characteristics of proteinsInternational Journal of Peptide and Protein Research, 1993
- Conformations of proline residues in membrane environmentsBiopolymers, 1990
- Prediction of protein structural class by discriminant analysisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Prediction of the Secondary Structure of Proteins from their Amino Acid SequencePublished by Wiley ,1979