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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, radiation, or heat. [3]

  3. 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 ...

  4. Chemical process of decomposition - Wikipedia

    en.wikipedia.org/wiki/Chemical_process_of...

    The human body is composed of approximately: 64% water, 20% protein, 10% fat, 1% carbohydrate, 5% minerals. [1] The decomposition of soft tissue is characterized by the breakdown of these macromolecules, and thus a large proportion of the decomposition products should reflect the amount of protein and fat content initially present in the body. [4]

  5. Protein aggregation - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation

    In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. [1] [2] Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion ...

  6. List of proteins - Wikipedia

    en.wikipedia.org/wiki/List_of_proteins

    At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]

  7. PSE meat - Wikipedia

    en.wikipedia.org/wiki/PSE_meat

    As the pH drops, proteins in the myofibers are denatured, leading to abnormal cell structure. The result is a pale tissue color, and a soft, almost mushy texture. The sarcomeres collapse excessively, and less water is held within the cell membrane and proteins. Subsequently, the myofibers will continue to lose water content as the meat is ...

  8. Luciferase - Wikipedia

    en.wikipedia.org/wiki/Luciferase

    Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein.The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. [1]

  9. Poikilotherm - Wikipedia

    en.wikipedia.org/wiki/Poikilotherm

    One of the most important stressors is outer environment temperature change, which can lead to alterations in membrane lipid order and can cause protein unfolding and denaturation at elevated temperatures. [1] Poikilotherm is the opposite of homeotherm – an animal which maintains thermal homeostasis.