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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. 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.

  4. Prion - Wikipedia

    en.wikipedia.org/wiki/Prion

    Sterilizing prions, therefore, requires the denaturation of the protein to a state in which the molecule is no longer able to induce the abnormal folding of normal proteins. In general, prions are quite resistant to proteases, heat, ionizing radiation, and formaldehyde treatments, [95] although their infectivity can be reduced by such treatments.

  5. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    A number of models have been proposed to explain this observation prominent among them being the denaturant binding model, solvent-exchange model (both by John Schellman [4]) and the Linear Extrapolation Model (LEM; by Nick Pace [5]). All of the models assume that only two thermodynamic states are populated/de-populated upon denaturation.

  6. Luciferase - Wikipedia

    en.wikipedia.org/wiki/Luciferase

    Luciferase is a heat-sensitive protein that is used in studies on protein denaturation, testing the protective capacities of heat shock proteins. The opportunities for using luciferase continue to expand. [29]

  7. Denaturation midpoint - Wikipedia

    en.wikipedia.org/wiki/Denaturation_midpoint

    Denaturation midpoint of a protein is defined as the temperature (T m) or concentration of denaturant (C m) at which both the folded and unfolded states are equally populated at equilibrium (assuming two-state protein folding). T m is often determined using a thermal shift assay.

  8. Particle number - Wikipedia

    en.wikipedia.org/wiki/Particle_number

    In thermodynamics, the particle number (symbol N) of a thermodynamic system is the number of constituent particles in that system. [1] The particle number is a fundamental thermodynamic property which is conjugate to the chemical potential. Unlike most physical quantities, the particle number is a dimensionless quantity, specifically a ...

  9. Nucleic acid thermodynamics - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_thermodynamics

    The process of DNA denaturation can be used to analyze some aspects of DNA. Because cytosine / guanine base-pairing is generally stronger than adenine / thymine base-pairing, the amount of cytosine and guanine in a genome is called its GC-content and can be estimated by measuring the temperature at which the genomic DNA melts. [2]