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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. 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.

  4. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    Since proteins typically aggregate upon denaturation (or form fibrils) the detected species size will go up. This is label-free and independent of specific residues in the protein or buffer composition. The only requirement is that the protein actually aggregates/fibrillates after denaturation and that the protein of interest has been purified.

  5. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.

  6. Helicase-dependent amplification - Wikipedia

    en.wikipedia.org/wiki/Helicase-dependent...

    The polymerase chain reaction is the most widely used method for in vitro DNA amplification for purposes of molecular biology and biomedical research. [1] This process involves the separation of the double-stranded DNA in high heat into single strands (the denaturation step, typically achieved at 95–97 °C), annealing of the primers to the single stranded DNA (the annealing step) and copying ...

  7. Polyacrylamide gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Polyacrylamide_gel...

    Picture of an SDS-PAGE. The molecular markers (ladder) are in the left lane. Polyacrylamide gel electrophoresis (PAGE) is a technique widely used in biochemistry, forensic chemistry, genetics, molecular biology and biotechnology to separate biological macromolecules, usually proteins or nucleic acids, according to their electrophoretic mobility.

  8. Southern blot - Wikipedia

    en.wikipedia.org/wiki/Southern_blot

    Southern blots performed with restriction enzyme-digested genomic DNA may be used to determine the number of sequences (e.g., gene copies) in a genome. A probe that hybridizes only to a single DNA segment that has not been cut by the restriction enzyme will produce a single band on a Southern blot, whereas multiple bands will likely be observed ...

  9. Hot start PCR - Wikipedia

    en.wikipedia.org/wiki/Hot_start_PCR

    In antibody based procedures, each enzyme requires a different antibody and therefore the cost to perform the procedure is higher. [15] There is also evidence that many commercial hot start enzymes actually have some level of activity prior to denaturation, and few suppliers provide any information about testing for this residual activity. [25]