Decrease in binding energy of Ste5 protein to membrane in each phosphorylation event

Range ~1.4 kcal/mol
Organism Unspecified
Reference Serber Z, Ferrell JE Jr. Tuning bulk electrostatics to regulate protein function. Cell. 2007 Feb 9 128(3):441-4. p.442 right column 2nd paragraphPubMed ID17289565
Comments "The essential features of McLaughlin’s model are found prominently in the regulation of Ste5's association with the plasma membrane. For Ste5, the role of myristoylation is played by the weak protein-protein interaction with the receptor-activated Gß? dimer. The multisite phosphorylation of Ste5 first weakens the association of Ste5 with the membrane and then ultimately reverses it. If the McLaughlin data apply, each Ste5 phosphorylation decreases the binding energy by (probably) about 1.4 kcal/mol." See BNID 105721
Entered by Uri M
ID 105724