Abstract
In multipass transmembrane proteins one face of the transmembrane helices is in contact with the aliphatic acyl chains of the phospholipids and with the polar interface region. The other face makes contacts with other helices or points into the protein interior. In larger proteins, some helices may even be buried completely. Analysis of the available three-dimensional crystal structures has shown that inwards pointing residues tend to be more conserved than outwards pointing residues. Furthermore, residues pointing outwards are generally very hydrophobic whereas inward pointing residues may have different characteristics. Based on these two findings, knowledge-based propensity scales have been derived that, when combined with analysis of residue conservation, allow predicting the exposure status of residues in the hydrophobic core region with about 80% accuracy. These tools give biologists insight in the putative topology of transmembrane helix bundles.
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Helms, V., Hayat, S., Metzger, J. (2010). Predicting the burial/exposure status of transmembrane residues in helical membrane proteins. In: Structural Bioinformatics of Membrane Proteins. Springer, Vienna. https://doi.org/10.1007/978-3-7091-0045-5_9
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DOI: https://doi.org/10.1007/978-3-7091-0045-5_9
Publisher Name: Springer, Vienna
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