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  2. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    The hydrolysis of a protein (red) by the nucleophilic attack of water (blue). The uncatalysed half-life is several hundred years. Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years.

  3. Heller's test - Wikipedia

    en.wikipedia.org/wiki/Heller's_test

    Concentrated nitric acid is added to a protein solution from the side of the test tube to form two layers. A white ring appears between the two layers if the test is positive. [1] Heller's test is commonly used to test for the presence of proteins in urine. [2] This test was discovered by the Austrian Chemist, Johann Florian Heller (1813-1871).

  4. 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]

  5. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    where is the stability of the protein in water and [D] is the denaturant concentration. Thus the analysis of denaturation data with this model requires 7 parameters: Δ G w {\displaystyle \Delta G_{w}} , Δ n {\displaystyle \Delta n} , k , and the slopes and intercepts of the folded and unfolded state baselines.

  6. Hydrophobic collapse - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic_collapse

    Correct protein folding is integral to proper functionality within biological systems. Hydrophobic collapse is one of the main events necessary for reaching a protein's stable and functional conformation. Proteins perform extremely specific functions which are dependent on their structure. Proteins that do not fold correctly are nonfunctional ...

  7. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Bio-layer interferometry (BLI) is a label-free technology for measuring biomolecular interactions [27] [28] (protein:protein or protein:small molecule). It is an optical analytical technique that analyzes the interference pattern of white light reflected from two surfaces: a layer of immobilized protein on the biosensor tip, and an internal ...

  8. Activated protein C resistance test - Wikipedia

    en.wikipedia.org/wiki/Activated_protein_C...

    The activated protein C resistance (APCR) test is a coagulation test used in the evaluation and diagnosis of activated protein C (APC) resistance, a form of hypercoagulability. [ 1 ] [ 2 ] Hereditary APC resistance is usually caused by the factor V Leiden mutation, whereas acquired APC resistance has been linked to antiphospholipid antibodies ...

  9. Thermostability - Wikipedia

    en.wikipedia.org/wiki/Thermostability

    Crystal structure of β-glucosidase from Thermotoga neapolitana (PDB: 5IDI).Thermostable protein, active at 80°C and with unfolding temperature of 101°C. [1]In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative ...