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  2. 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).

  3. 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]

  4. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    The system does not require solvatochromic dyes, reducing the risk of interferences. The protein samples are simply mixed with the test conditions in a 96-well plate and subjected to a melt-curve protocol using a real-time thermal cycler. The data are obtained within 1–2 h and include unique quality control measures through the GFP signal.

  5. Methods to investigate protein–protein interactions - Wikipedia

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

    Whereas the concept of water activity is widely known and utilized in the applied biosciences, its complement—the protein activity which quantitates proteinprotein interactions—is much less familiar to bioscientists as it is more difficult to determine in dilute solutions of proteins; protein activity is also much harder to determine for ...

  6. 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 ...

  7. Albumin - Wikipedia

    en.wikipedia.org/wiki/Albumin

    Albumin is a family of globular proteins, the most common of which are the serum albumins. All of the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not ...

  8. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    This differential scale has two comparative advantages: (1) it is especially useful for treating changes in water-protein interactions that are too small to be accessible to conventional force-field calculations, and (2) for homologous structures, it can yield correlations with changes in properties from mutations in the amino acid sequences ...

  9. Contact activation system - Wikipedia

    en.wikipedia.org/wiki/Contact_activation_system

    The two arms of the contact system. PKa's cleavage of HK liberates BK and promotes inflammation. FXIIa's cleavage of FXI initiates coagulation. In the contact activation system or CAS, three proteins in the blood, factor XII (FXII), prekallikrein (PK) and high molecular weight kininogen (HK), bind to a surface and cause blood coagulation and ...