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The pH of a salt solution is determined by its component anions and cations. Salts that contain pH-neutral anions and the hydronium ion-producing cations form a solution with a pH less than 7. For example, in ammonium nitrate (NH4NO3) solution, NO3− ions do not react with water whereas NH4+ ions produce the hydronium ions resulting in the acidic solution.  In contrast, salts that contain pH-neutral cations and the hydroxide ion-producing anions form a solution with a pH greater than...
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Consider a neutral form of an amine, B, with a partition coefficient, K, in a liquid mixture containing organic and aqueous phases. The pH of the aqueous phase affects the charge on acidic and basic solutes, and the charged form is usually more soluble in the aqueous phase. Suppose the conjugate acid form of the amine is soluble only in the aqueous phase while the base form is soluble in both phases. Then the distribution coefficient, D, can be given as the ratio of amine concentration in the...
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Drug absorption within the gastrointestinal (GI) tract is a complex process influenced by several critical factors, including the site pH, the drug's dissociation constant (pKa), and the drug's lipophilicity. The GI tract exhibits a pH gradient, with an acidic environment in the stomach and a more alkaline environment in the small intestine. This pH variation directly affects the ionization state of drugs.
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Solubility equilibria are established when the dissolution and precipitation of a solute species occur at equal rates. These equilibria underlie many natural and technological processes, ranging from tooth decay to water purification. An understanding of the factors affecting compound solubility is, therefore, essential to the effective management of these processes. This section applies previously introduced equilibrium concepts and tools to systems involving dissolution and precipitation.
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Updated: Aug 12, 2025

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
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Sequence-based prediction of pH-dependent protein solubility using CamSol.

Marc Oeller1, Ryan Kang1, Rosie Bell1

  • 1Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.

Briefings in Bioinformatics
|January 31, 2023
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Summary

A new computational method predicts protein solubility, including pH effects, with accuracy matching experimental techniques. This tool aids rapid screening for biotechnology and medicine applications.

Keywords:
developabilitydrug formulationpH dependencyprotein solubilitysolubility prediction

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Area of Science:

  • Biochemistry
  • Biotechnology
  • Computational Biology

Background:

  • Protein solubility is crucial for molecular biology research, biotechnology, and medicine.
  • Experimental solubility measurements are time-consuming and resource-intensive.
  • Computational methods offer rapid, cost-effective screening for protein development.

Purpose of the Study:

  • To develop a computational method for predicting protein solubility.
  • To incorporate the influence of pH on protein solubility predictions.
  • To provide a tool for efficient screening of protein solubility in large libraries.

Main Methods:

  • Development of a pH-dependent computational solubility prediction model.
  • Testing the model on diverse proteins, including antibodies.
  • Validation of prediction accuracy against experimental data.

Main Results:

  • The developed method accurately predicts pH-dependent protein solubility.
  • Prediction accuracy is comparable to experimental measurement methods.
  • The tool demonstrates reliable performance across various protein types.

Conclusions:

  • The new computational method enhances protein solubility prediction by including pH effects.
  • This tool supports rapid and accurate screening in protein engineering and development pipelines.
  • The pH-dependent solubility prediction method is publicly available as CamSol v3.0.