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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. SDD-AGE - Wikipedia

    en.wikipedia.org/wiki/SDD-AGE

    In biochemistry and molecular biology, SDD-AGE is short for Semi-Denaturating Detergent Agarose Gel Electrophoresis. This is a method for detecting and characterizing large protein polymers which are stable in 2% SDS at room temperature, unlike most large protein complexes.

  4. Acid guanidinium thiocyanate-phenol-chloroform extraction

    en.wikipedia.org/wiki/Acid_guanidinium...

    Guanidinium thiocyanate, a chaotropic agent, is added to the organic phase to aid in the denaturation of proteins (such as those that strongly bind nucleic acids or those that degrade RNA). The nucleic acids ( RNA and/or DNA ) partition into the aqueous phase, while protein partitions into the organic phase.

  5. 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.

  6. Lysis buffer - Wikipedia

    en.wikipedia.org/wiki/Lysis_buffer

    The primary purpose of lysis buffer is isolating the molecules of interest and keeping them in a stable environment. For proteins, for some experiments, the target proteins should be completely denatured, while in some other experiments the target protein should remain folded and functional. Different proteins also have different properties and ...

  7. 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.

  8. Study: 21 popular cereals found to have cancer-linked Roundup ...

    www.aol.com/lifestyle/study-21-popular-cereals...

    New tests done by the Environmental Working Group have found 21 oat-based cereals and snack bars popular amongst children to have "troubling levels of glyphosate." The chemical, which is the ...

  9. Temperature gradient gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Temperature_gradient_gel...

    The process of denaturation on a denaturing gel is very sharp: "Rather than partially melting in a continuous zipper-like manner, most fragments melt in a step-wise process. Discrete portions or domains of the fragment suddenly become single-stranded within a very narrow range of denaturing conditions" (Helms, 1990).

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