Number of CH2 units of a myristoylated protein embedded into the hydrocarbon interior of the membrane

Value 10 unitless
Organism Generic
Reference McLaughlin S, Aderem A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem Sci. 1995 Jul20(7):272-6. p.272 right column bottom linePubMed ID7667880
Comments The slope of 0.8 kcal/mol per CH2 group is similar to that observed by Tanford (ref 17) for the partitioning of the neutral form of a fatty acid from water into a bulk alkane phase. Myristoylated glycine (myr-G) myr-GA, myrGAA and a myristoylated peptide corresponding to the first 15 residues of Src (see Fig. 1) all bind with a unitary Gibbs free energy of ?Gu=-8 kcal/mol into the hydrocarbon interior of the membrane to electrically neutral vesicles. This implies that about 8/0.8 = 10 CH2 groups are removed from water and embedded into the hydrocarbon interior of the membrane.
Entered by Uri M
ID 105720