Molecular-Level Thermodynamic Switch Controls Chemical Equilibrium in Sequence-Specific Hydrophobic Interaction of 35 Dipeptide Pairs

摘要: Abstract Applying the Planck-Benzinger methodology, sequence-specific hydrophobic interactions of 35 dipeptide pairs were examined over a temperature range 273–333K, based on data reported by Nemethy and Scheraga in 1962. The interaction these is highly similar its thermodynamic behavior to that other biological systems. results imply negative Gibbs free energy change minimum at well-defined stable temperature, 〈 T s 〉, where bound unavailable energy, Δ S o =0, has origin interactions, are dependent details molecular structure. Each case confirms existence switch wherein sign Cp ( ) reaction (change specific heat capacity constant pressure) leads true reaction, G , hence maximum related equilibrium constant, K eq . Indeed, all interacting systems date Chun using methodology have shown such level, suggesting may be universal.