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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. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids.

  4. Anfinsen's dogma - Wikipedia

    en.wikipedia.org/wiki/Anfinsen's_dogma

    Folded, 3-D structure of ribonuclease A. Anfinsen's dogma, also known as the thermodynamic hypothesis, is a postulate in molecular biology.It states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence. [1]

  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. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases.. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney.

  7. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    Chaperone proteins participate in the folding of over half of all mammalian proteins. [citation needed] Macromolecular crowding may be important in chaperone function. The crowded environment of the cytosol can accelerate the folding process, since a compact folded protein will occupy less volume than an unfolded protein chain. [9]

  8. The Fastest Way to Debloat After a Big Meal, According to ...

    www.aol.com/fastest-way-debloat-big-meal...

    In fact, according to San Diego-based registered dietitian and ACSM-certified exercise physiologist Wendy Bazilian, Dr.P.H., M.A., RDN, “Gentle movement, like a post-meal walk, stimulates the ...

  9. Maillard reaction - Wikipedia

    en.wikipedia.org/wiki/Maillard_reaction

    In archaeology, the Maillard process occurs when bodies are preserved in peat bogs. The acidic peat environment causes a tanning or browning of skin tones and can turn hair to a red or ginger tone. The chemical mechanism is the same as in the browning of food, but it develops slowly over time due to the acidic action on the bog body.