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Identification of transmembrane helicesEdit
Transmembrane helices are visible in structures of membrane proteins determined by X-ray diffraction. They may also be predicted on the basis of hydrophobicity scales. Because the interior of the bilayer and the interiors of most proteins of known structure are hydrophobic, it is presumed to be a requirement of the amino acids that span a membrane that they be hydrophobic as well. However, membrane pumps and ion channels also contain numerous charged and polar residues within the generally non-polar transmembrane segments.
Using hydrophobicity analysis to predict transmembrane helices enables a prediction in turn of the "transmembrane topology" of a protein; i.e. prediction of what parts of it protrude into the cell, what parts protrude out, and how many times the protein chain crosses the membrane.
- Tetraspanins have 4 conserved transmembrane domains.
- Hayley J. Sharpe; Tim J. Stevens; Sean Munro (9 July 2010). "A Comprehensive Comparison of Transmembrane Domains Reveals Organelle-Specific Properties". Cell. 142 (1): 158–169. doi:10.1016/j.cell.2010.05.037.