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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

    The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids. A by-product of this bond formation is the release of water (the amino group donates a proton while the carboxyl group donates a hydroxyl). [2]

  4. Chaperone (protein) - Wikipedia

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

    Bulk biochemical measurements have informed us on the protein folding efficiency, and prevention of aggregation when chaperones are present during protein folding. Recent advances in single-molecule analysis [ 3 ] have brought insights into structural heterogeneity of chaperones, folding intermediates and affinity of chaperones for unstructured ...

  5. Carbohydrate metabolism - Wikipedia

    en.wikipedia.org/wiki/Carbohydrate_metabolism

    Carbohydrates are typically stored as long polymers of glucose molecules with glycosidic bonds for structural support (e.g. chitin, cellulose) or for energy storage (e.g. glycogen, starch). However, the strong affinity of most carbohydrates for water makes storage of large quantities of carbohydrates inefficient due to the large molecular ...

  6. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.

  7. 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.

  8. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    A biomolecule or biological molecule is loosely defined as a molecule produced by a living organism and essential to one or more typically biological processes. [1] Biomolecules include large macromolecules such as proteins , carbohydrates , lipids , and nucleic acids , as well as small molecules such as vitamins and hormones.

  9. Glycoconjugate - Wikipedia

    en.wikipedia.org/wiki/Glycoconjugate

    Generally, the carbohydrate part(s) play an integral role in the function of a glycoconjugate; prominent examples of this are neural cell adhesion molecule (NCAM) and blood proteins where fine details in the carbohydrate structure determine cell binding (or not) or lifetime in circulation.