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  2. Denaturation (biochemistry) - Wikipedia

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

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Denaturation - Wikipedia

    en.wikipedia.org/wiki/Denaturation

    Denaturation (biochemistry), a structural change in macromolecules caused by extreme conditions; Denaturation (fissile materials), transforming fissile materials so that they cannot be used in nuclear weapons; Denaturation (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses

  4. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    Since proteins typically aggregate upon denaturation (or form fibrils) the detected species size will go up. This is label-free and independent of specific residues in the protein or buffer composition. The only requirement is that the protein actually aggregates/fibrillates after denaturation and that the protein of interest has been purified.

  5. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Many allergies are caused by the incorrect folding of some proteins because the immune system does not produce the antibodies for certain protein structures. [5] Denaturation of proteins is a process of transition from a folded to an unfolded state. It happens in cooking, burns, proteinopathies, and other contexts. Residual structure present ...

  6. Protein denaturation - Wikipedia

    en.wikipedia.org/?title=Protein_denaturation&...

    This page was last edited on 7 October 2005, at 21:54 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may ...

  7. Collagen hybridizing peptide - Wikipedia

    en.wikipedia.org/wiki/Collagen_Hybridizing_Peptide

    Schematic of a CHP strand (labeled with an "X" tag) hybridizing to denatured collagen chains and forming a collagen triple helix. During disease progression, tissue development, or ageing, collagen can be extensively degraded by collagenolytic proteases, causing its triple helix to unfold at the physiological temperature due to reduced thermal stability.

  8. Cyclol - Wikipedia

    en.wikipedia.org/wiki/Cyclol

    Nevertheless, protein scientists could not exclude the possibility that denaturation corresponded to a chemical change in the protein structure, [19] a hypothesis that was considered a (distant) possibility until the 1950s.

  9. Protein engineering - Wikipedia

    en.wikipedia.org/wiki/Protein_engineering

    Protein engineering is the process of developing useful or valuable proteins through the design and production of unnatural polypeptides, often by altering amino acid sequences found in nature. [1] It is a young discipline, with much research taking place into the understanding of protein folding and recognition for protein design principles.