Open AccessOn the attribution and additivity of binding energies
Author(s) -
William P. Jencks
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.7.4046
Subject(s) - gibbs free energy , additive function , binding energy , chemistry , molecule , binding site , computational chemistry , thermodynamics , biochemistry , physics , mathematics , organic chemistry , atomic physics , mathematical analysis
It can be useful to describe the Gibbs free energy changes for the binding to a protein of a molecule, A—B, and of its component parts, A and B, in terms of the “intrinsic binding energies” of A and B, ΔG A i and ΔG B i , and a “connection Gibbs energy,” ΔG s that is derived largely from changes in translational and rotational entropy. This empirical approach avoids the difficult or insoluble problem of interpreting observed ΔH andT ΔS values for aqueous solutions. The ΔG i and ΔG s terms can be large for binding to enzymes and other proteins.