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Related Concept Videos

Adsorption Isotherms I01:29

Adsorption Isotherms I

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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...
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Adsorption Isotherms II01:25

Adsorption Isotherms II

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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...
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Adsorption of Gases on Solids01:28

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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...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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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...
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Monitoring Protein Adsorption with Solid-state Nanopores
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Temperature-driven adsorption and desorption of proteins at solid-liquid interfaces.

Irena Kiesel1, Michael Paulus, Julia Nase

  • 1Fakultät Physik/DELTA, Technische Universität Dortmund , 44221 Dortmund, Germany.

Langmuir : the ACS Journal of Surfaces and Colloids
|February 25, 2014
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Summary

Heat affects protein layers, causing desorption in buffer and adsorption in protein solutions. Protein mobility and conformational changes drive these surface interactions, influencing biofilm formation.

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Area of Science:

  • Biophysics
  • Surface Chemistry
  • Materials Science

Background:

  • Protein adsorption at interfaces is crucial for biological processes and material science.
  • Understanding heat-induced protein behavior is key to controlling surface interactions.
  • Existing models often lack a clear distinction between thermodynamic and kinetic drivers of protein adsorption.

Purpose of the Study:

  • To investigate heat-induced desorption and adsorption of specific proteins (lysozyme, ribonuclease A, bovine serum albumin, fibronectin) at protein layers.
  • To differentiate between thermodynamic and kinetic mechanisms governing protein adsorption using two distinct environments (pure buffer and protein solution).
  • To elucidate the factors influencing protein mobility and conformational changes at solid-liquid interfaces.

Main Methods:

  • Investigated heat-induced protein desorption and adsorption using model proteins.
  • Utilized two environments: pure buffer and protein solution, to isolate mechanisms.
  • Analyzed protein properties such as size, stability, and charge to correlate with observed behaviors.

Main Results:

  • Observed protein desorption in pure buffer and adsorption in protein solution.
  • Demonstrated that protein properties (size, stability, charge) dictate the adsorption/desorption behavior.
  • Identified protein mobility at the interface as the primary driver for desorption in buffer.
  • Concluded that conformational changes leading to entropy gain drive adsorption in protein solution.

Conclusions:

  • Desorption in buffer is primarily governed by protein interfacial mobility.
  • Adsorption in protein solution is driven by protein conformational changes and entropic gains.
  • These findings provide insights for controlling protein behavior at solid-liquid interfaces, relevant to biofilm formation.