Tympanic part of the temporal bone presents a narrow furrow, the "tympanic sulcus", for the attachment of the tympanic membrane. Its antero-inferior surface is quadrilateral and slightly concave; it constitutes the posterior boundary of the mandibular fossa, and is in contact with the retromandibular part of the parotid gland. Its lateral border is free and rough, and gives attachment to the cartilaginous part of the ear canal. Internally, the tympanic part is fused with the petrous portion, and appears in the retreating angle between it and the squama, where it lies below and lateral to the orifice of the auditory tube. Posteriorly, it blends with the
Membrane curvature several amphipathic alpha helices that allows it to partition between the hydrophobic core of the membrane and surrounding aqueous, hydrophilic environment. Another interesting characteristic of epsin and other proteins that bind to membranes is the fact that it shows high binding affinity for a fairly common membrane lipid, phosphatidylinositol 4,5-bisphosphate (PI-4,5-P2). Unlike other proteins that simply bend the membrane through sheer rigidity, epsin is a globular soluble protein and thus not rigid. The insertion of its helices into the membrane force the neighboring lipids of the leaflet that has been bound to expand laterally. This displacement of lipids on only