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Adsorption Isotherms I

Adsorption Isotherms I

Adsorption isotherms are mathematical models that describe how molecules in a gas or liquid phase interact with surfaces. Two of the most common isotherm models are the Langmuir and Freundlich isotherms, which relate to Type I monolayer chemisorption. The Langmuir model is based on four key assumptions:• Adsorption cannot exceed monolayer coverage.• All surface sites are equivalent.• Molecules adsorb only at vacant sites.• There are no interactions between adsorbed molecules.Consider the...

Adsorption of Gases on Solids

Adsorption of Gases on Solids

Adsorption is a process where molecules, known as the adsorbates, accumulate on a surface, which is referred to as the adsorbent or substrate. Occurring at the solid-gas interface, this phenomenon is crucial in various scientific and industrial contexts. The reverse of adsorption is desorption.Two types of adsorptions exist: physical (physisorption) and chemical (chemisorption). Physisorption involves gas molecules held to the solid's surface by relatively weak intermolecular van der Waals...

Adsorption Isotherms II

Adsorption Isotherms II

Brunauer, Emmett, and Teller (BET) introduced a theory in 1938 that modified Langmuir's assumptions to explain multilayer physical adsorption. This theory is applicable to Type II isotherms and provides a more realistic picture of adsorption processes. The BET theory assumes a uniform solid surface with localized adsorption sites, where adsorption at one site doesn't affect adsorption at neighboring sites. This theory also allows for the possibility of additional molecules being adsorbed on top...

Analyte Adsorption and Distribution

Analyte Adsorption and Distribution

In certain chromatographic separations, solutes transfer between the mobile phase and the stationary phase via sorption, which typically refers to the process of adsorption. For many chromatographic systems, the sorption process often depends on the polarity of the compounds—an expression of the overall dipole moment within the molecule. During the separation process, there is competition between the solute and solvent for adsorption to the stationary phase. Highly polar compounds and solvents...

Heterogeneous Catalysis

Heterogeneous Catalysis

Heterogeneous catalysis involves a catalyst in a different phase from the reactants. It is a process where the catalyst and the reactants are in distinct phases, typically solid and gas or liquid.Most heterogeneous catalysts are metals, metal oxides, or acids. The list includes transition metals like iron (Fe), cobalt (Co), nickel (Ni), palladium (Pd), platinum (Pt), chromium (Cr), manganese (Mn), tungsten (W), silver (Ag), and copper (Cu). These metals possess partially vacant d orbitals that...

Affinity Chromatography

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...

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Related Experiment Video

Updated: Jun 25, 2026

Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Inhomogeneity of adsorbed proteins on a solid surface.

¹Chemical and Biological Engineering, Missouri University of Science and Technology, Rolla, MO 65409-1230, United States. neogi@mst.edu

Colloids and Surfaces. B, Biointerfaces

|February 24, 2009

Summary

Protein adsorption on charged surfaces leads to non-uniform clustering. Electrostatic forces drive this instability, with cluster growth rate depending on protein and surface charges.

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Monitoring Protein Adsorption with Solid-state Nanopores

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Published on: December 2, 2011

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Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

Published on: February 27, 2015

Area of Science:

Physical Chemistry
Surface Science
Biophysics

Background:

Proteins adsorb non-uniformly on solid surfaces, forming clusters.
Previous studies ruled out bulk clustering and adsorbed phase changes in dilute, irreversible adsorption systems.

Purpose of the Study:

To investigate the causes of protein clustering during irreversible adsorption on charged surfaces.
To analyze the stability of protein adsorption under diffusion-limited conditions.

Main Methods:

Developed an approximate solution for the non-equilibrium double layer in diffusion-limited adsorption.
Performed a linear stability analysis of the adsorption process.

Main Results:

Protein adsorption on charged surfaces is inherently unstable to small perturbations.
Electrostatic attraction between proteins and the charged substrate overcomes small positional disturbances.
The rate of cluster formation is directly proportional to the protein charge and substrate surface charge density.

Conclusions:

Electrostatic interactions are the primary drivers of protein clustering during irreversible adsorption.
The observed inhomogeneity in protein adsorption is a consequence of surface instability.
Understanding these forces is crucial for controlling protein assembly on surfaces.