Epidermal growth factor receptor transmembrane domain: 2H NMR implications for orientation and motion in a bilayer environment

A study relating to the investigation of the function of receptor tyrosine kinases was conducted to specifically scrutinize spectral data from three alamine residues within the putative transmembrane domain using H NMR spectroscopy. Experimental data strongly suggests that the peptide long axis tilts at an angle of between 10 and 14 degrees in fluid membranes of 1-palmitoyl-2-oleophosphatidylcholine (POPC) and between 10 and 12 degrees in POPC/cholesterol assuming that the transmembrane domain of the human EGF receptor is required to be a right-handed alpha-helix of 3.6 residues per turn.