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5_60_lecture17

5_60_lecture17 - MIT OpenCourseWare http/ocw.mit.edu 5.60...

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MIT OpenCourseWare http://ocw.mit.edu 5.60 Thermodynamics & Kinetics Spring 2008 For information about citing these materials or our Terms of Use, visit: http://ocw.mit.edu/terms .
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5.60 Spring 2008 Lecture #17 page 1 Equilibrium: Application to Drug Design Based on “Rational cytokine design for increased lifetime and enhanced potency using pH-activated histidine switching,” Sarkar, Lowenhaupt, Horan, Boone, Tidor, and Lauffenburger, Nature Biotechnology 20 , 908 (2002). The analysis for equilibrium that we have used for reactions involving breaking and making covalent bonds applies equally well to reactions such as those involved in ligand-receptor binding, where the ligand and receptor are proteins R + L = C where R is the receptor, L is the ligand, and C is the receptor-ligand complex. The interactions between these proteins typically involve multiple non-covalent interactions, including hydrogen bonds, hydrophobic interactions, and electrostatic interactions. The equilibrium constant and Gibbs free energy change for the reaction are related in the usual way = − ln o a G RT K where the equilibrium constant K a is called the association constant [ ] [ ][ ] = a C K R L The standard state needed to characterize o G
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