Biogeosciences Temperature , pressure , and electrochemical constraints on protein speciation : Group additivity calculation of the standard molal thermodynamic properties of ionized unfolded proteins

@inproceedings{Dick2006BiogeosciencesT,
  title={Biogeosciences Temperature , pressure , and electrochemical constraints on protein speciation : Group additivity calculation of the standard molal thermodynamic properties of ionized unfolded proteins},
  author={Jeffrey M. Dick and Douglas E Larowe and Harold C. Helgeson},
  year={2006}
}
Thermodynamic calculations can be used to quantify environmental constraints on the speciation of proteins, such as the pH and temperature dependence of ionization state, and the relative chemical stabilities of proteins in different biogeochemical settings. These calculations depend in part on values of the standard molal Gibbs energies of proteins and their ionization reactions as a function of temperature and pressure. Because these values are not generally available, we calculated values of… CONTINUE READING
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