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MPRAP: An accessibility predictor for a-helical transmem-brane proteins that performs well inside and outside the membrane
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-7115-9751
2010 (English)In: BMC Bioinformatics, ISSN 1471-2105, Vol. 11, 333- p.Article in journal (Refereed) Published
Abstract [en]

Background: In water-soluble proteins it is energetically favorable to bury hydrophobic residues and to expose polar and charged residues. In contrast to water soluble proteins, transmembrane proteins face three distinct environments; a hydrophobic lipid environment inside the membrane, a hydrophilic water environment outside the membrane and an interface region rich in phospholipid head-groups. Therefore, it is energetically favorable for transmembrane proteins to expose different types of residues in the different regions. Results: Investigations of a set of structurally determined transmembrane proteins showed that the composition of solvent exposed residues differs significantly inside and outside the membrane. In contrast, residues buried within the interior of a protein show a much smaller difference. However, in all regions exposed residues are less conserved than buried residues. Further, we found that current state-of-the-art predictors for surface area are optimized for one of the regions and perform badly in the other regions. To circumvent this limitation we developed a new predictor, MPRAP, that performs well in all regions. In addition, MPRAP performs better on complete membrane proteins than a combination of specialized predictors and acceptably on water-soluble proteins. A web-server of MPRAP is available at Conclusion: By including complete a-helical transmembrane proteins in the training MPRAP is able to predict surface accessibility accurately both inside and outside the membrane. This predictor can aid in the prediction of 3D-structure, and in the identification of erroneous protein structures.

Place, publisher, year, edition, pages
2010. Vol. 11, 333- p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-49473DOI: 10.1186/1471-2105-11-333ISI: 000280332100001OAI: diva2:377960
EU, FP7, Seventh Framework Programme, 512092Swedish Foundation for Strategic Research

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Available from: 2010-12-15 Created: 2010-12-14 Last updated: 2014-11-10Bibliographically approved

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Illergård, KristofferElofsson, Arne
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