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A Review of the Thermodynamics of Protein Association to Ligands, Protein Adsorption, and Adsorption Isotherms

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Hydrophobic displacement chromatography of proteins
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Steric mass‐action ion exchange: Displacement profiles and induced salt gradients
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Galenics of Insulin
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Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series
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Gibbs free energy of adsorption for biomolecules in ion-exchange systems
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Linear Chromatography
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Effect of pH changes on water release values in hydrophobic interaction chromatographic systems
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Generalizing a two-conformation model for describing salt and temperature effects on protein retention and stability in hydrophobic interaction chromatography
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Quality by design—Thermodynamic modelling of chromatographic separation of proteins
inferredcites →https://doi.org/10.1016/j.chroma.2007.09.031openalex-snapshot
Thermodynamics of hydrophobic interaction chromatography of acetyl amino acid methyl esters
inferredcites →https://doi.org/10.1016/j.chroma.2007.11.003openalex-snapshot
Prediction of protein retention times in gradient hydrophobic interaction chromatographic systems
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Applied thermodynamics: A new frontier for biotechnology
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Development, modelling, optimisation and scale-up of chromatographic purification of a therapeutic protein
inferredcites →https://doi.org/10.1016/j.jbiotec.2007.05.036openalex-snapshot
The thermodynamic principles of ligand binding in chromatography and biology
inferredcites →https://doi.org/10.1016/s0021-9673(01)88960-3openalex-snapshot
Gradient elution in non-linear preparative liquid chromatography
inferredcites →https://doi.org/10.1016/s0021-9673(02)02047-2openalex-snapshot
Modeling of adsorption in hydrophobic interaction chromatography systems using a preferential interaction quadratic isotherm
inferredcites →https://doi.org/10.1016/s1570-0232(03)00127-2openalex-snapshot
Whey proteins as a model system for chromatographic separation of proteins
inferredcites →https://doi.org/10.1021/bp049712+openalex-snapshot
Protein Interactions in Hydrophobic Charge Induction Chromatography (HCIC)
inferredcites →https://doi.org/10.1021/ie9507437openalex-snapshot
Retention Thermodynamics in Hydrophobic Interaction Chromatography
inferredcites →https://doi.org/10.1351/pac199365040819openalex-snapshot
Nomenclature for chromatography (IUPAC Recommendations 1993)

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Modeling of salt and pH gradient elution in ion‐exchange chromatography
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Hydrophobic interaction chromatography of proteins: Thermodynamic analysis of conformational changes
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Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography
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Continuous Biopharmaceutical Processes
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Preface
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Introduction to Biopharmaceutical Processes
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Fundamentals of Protein Chromatography
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Countercurrrent Separation Processes
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Countercurrent Chromatography for the Capture Step
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Countercurrent Chromatography for the Polishing Steps
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Protein Conjugation
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Protein Aggregation in Biopharmaceutical Processes
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Conclusion
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Bibliography
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Index
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Contribution à la compréhension de la chromatographie d'échange d'ions des protéines par un couplage d'approches expérimentales et de simulations moléculaires.
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