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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. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Denaturation of proteins is a process of transition from a folded to an unfolded state. It happens in cooking , burns , proteinopathies , and other contexts. Residual structure present, if any, in the supposedly unfolded state may form a folding initiation site and guide the subsequent folding reactions.

  5. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    The active site is located in the linkage between two subunits. The NADPH is involved in the generation of FADH-. In the active site, there are two cysteine residues besides the FAD cofactor and are used to break the disulphide bond during the catalytic reaction. NADPH is bound by three positively charged residues: Arg-218, His-219 and Arg-224.

  6. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    The most famous example is the hyperchromicity of DNA that occurs when the DNA duplex is denatured. [1] The UV absorption is increased when the two single DNA strands are being separated, either by heat or by addition of denaturant or by increasing the pH level. The opposite, a decrease of absorbance is called hypochromicity.

  7. Egg white - Wikipedia

    en.wikipedia.org/wiki/Egg_white

    Denaturation temperature is around 84 °C, but it can be easily denatured by physical stresses. Conalbumin/ovotransferrin is a glycoprotein which has the capacity to bind the bi- and trivalent metal cations into a complex and is more heat sensitive than ovalbumin. At its isoelectric pH (6.5), it can bind two cations and assume a red or yellow ...

  8. 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 ]

  9. Deoxyribonuclease - Wikipedia

    en.wikipedia.org/wiki/Deoxyribonuclease

    Two of the sites strongly bind Ca 2+ while the other two coordinate Mg 2+. Little has been published on the number and location of the Mg 2+ binding sites, although it has been proposed that Mg 2+ is located near the catalytic pocket and contributes to hydrolysis. [6] The two Ca 2+ are shown in red in the image. They are bound to DNase I under ...