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  2. Protein adsorption - Wikipedia

    en.wikipedia.org/wiki/Protein_adsorption

    Proteins are pH-dependent polyampholytes that undergo structural rearrangements upon adsorption, wherefore their adsorption depends on the protein thermodynamic stability, [37] the pH and ionic strength of the aqueous phase, [38] and the polarity of the respective phases. [39]

  3. Langmuir adsorption model - Wikipedia

    en.wikipedia.org/wiki/Langmuir_adsorption_model

    The Freundlich isotherm is the most important multi-site adsorption isotherm for rough surfaces. =, where α F and C F are fitting parameters. [14] This equation implies that if one makes a log–log plot of adsorption data, the data will fit a straight line. The Freundlich isotherm has two parameters, while Langmuir's equations has only one ...

  4. Adsorption - Wikipedia

    en.wikipedia.org/wiki/Adsorption

    Protein adsorption is a process that has a fundamental role in the field of biomaterials. Indeed, biomaterial surfaces in contact with biological media, such as blood or serum, are immediately coated by proteins. Therefore, living cells do not interact directly with the biomaterial surface, but with the adsorbed proteins layer.

  5. Molar absorption coefficient - Wikipedia

    en.wikipedia.org/wiki/Molar_absorption_coefficient

    In biochemistry, the molar absorption coefficient of a protein at 280 nm depends almost exclusively on the number of aromatic residues, particularly tryptophan, and can be predicted from the sequence of amino acids. [6] Similarly, the molar absorption coefficient of nucleic acids at 260 nm can be predicted given the nucleotide sequence.

  6. Henry adsorption constant - Wikipedia

    en.wikipedia.org/wiki/Henry_adsorption_constant

    Source: [2] If a solid body is modeled by a constant field and the structure of the field is such that it has a penetrable core, then = ′ [⁡ ⁡ ()] ′ [⁡ ()]. Here ′ is the position of the dividing surface, = is the external force field, simulating a solid, is the field value deep in the solid, = /, is the Boltzmann constant, and is the temperature.

  7. Hill equation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Hill_equation_(biochemistry)

    Protein-ligand binding typically changes the structure of the target protein, thereby changing its function in a cell. The distinction between the two Hill equations is whether they measure occupancy or response. The Hill equation reflects the occupancy of macromolecules: the fraction that is saturated or bound by the ligand.

  8. We all need HGH, the hormone responsible for growth. What ...

    www.aol.com/hgh-hormone-responsible-growth...

    In children, HGH stimulates linear growth and protein synthesis. It also helps with the breakdown of lipids fat, says O’Sullivan. In adults, HGH helps regulate blood glucose levels, she adds.

  9. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    The model is used in a variety of biochemical situations other than enzyme-substrate interaction, including antigen–antibody binding, DNA–DNA hybridization, and proteinprotein interaction. [ 17 ] [ 18 ] It can be used to characterize a generic biochemical reaction, in the same way that the Langmuir equation can be used to model generic ...