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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. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    Homeostatic control can change the P CO 2 and hence the pH of the arterial plasma within a few seconds. [5] The partial pressure of carbon dioxide in the arterial blood is monitored by the central chemoreceptors of the medulla oblongata. [5] [20] These chemoreceptors are sensitive to the levels of carbon dioxide and pH in the cerebrospinal ...

  4. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  5. 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]

  6. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    A thermal shift assay (TSA) measures changes in the thermal denaturation temperature and hence stability of a protein under varying conditions such as variations in drug concentration, buffer formulation (pH or ionic strength), redox potential, or sequence mutation. The most common method for measuring protein thermal shifts is differential ...

  7. Intracellular pH - Wikipedia

    en.wikipedia.org/wiki/Intracellular_pH

    The pH i plays a critical role in membrane transport and other intracellular processes. In an environment with the improper pH i, biological cells may have compromised function. [1] [2] Therefore, pH i is closely regulated in order to ensure proper cellular function, controlled cell growth, and normal cellular processes. [3]

  8. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    The hyperchromic effect is the striking increase in absorbance of DNA upon denaturation. The two strands of DNA are bound together mainly by the stacking interactions, hydrogen bonds and hydrophobic effect between the complementary bases. The hydrogen bond limits the resonance of the aromatic ring so the absorbance of the sample is limited as well.

  9. Transport protein - Wikipedia

    en.wikipedia.org/wiki/Transport_protein

    A transport protein (variously referred to as a transmembrane pump, transporter, escort protein, acid transport protein, cation transport protein, or anion transport protein) is a protein that serves the function of moving other materials within an organism. Transport proteins are vital to the growth and life of all living things.