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  2. 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.

  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. 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).

  5. Gel electrophoresis of nucleic acids - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis_of...

    Similarly, RNA and single-stranded DNA can be run and visualised by PAGE gels containing denaturing agents such as urea. PAGE gels are widely used in techniques such as DNA foot printing, EMSA and other DNA-protein interaction techniques. The measurement and analysis are mostly done with a specialized gel analysis software.

  6. Gel electrophoresis of proteins - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis_of...

    SDS is a strong detergent agent used to denature native proteins to unfolded, individual polypeptides. When a protein mixture is heated to 100 °C in presence of SDS, the detergent wraps around the polypeptide backbone. In this process, the intrinsic charges of polypeptides becomes negligible when compared to the negative charges contributed by ...

  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. Guanidinium thiocyanate - Wikipedia

    en.wikipedia.org/wiki/Guanidinium_thiocyanate

    Guanidinium thiocyanate can be used to deactivate a virus, such as the influenza virus that caused the 1918 "Spanish flu", so that it can be studied safely.. Guanidinium thiocyanate is also used to lyse cells and virus particles in RNA and DNA extractions, where its function, in addition to its lysing action, is to prevent activity of RNase enzymes and DNase enzymes by denaturing them.

  9. 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 ...