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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. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    A known result of cytosine methylation is the increase of C-to-T transition mutations through the process of deamination. Cytosine deamination can alter the genome's many regulatory functions; previously silenced transposable elements (TEs) may become transcriptionally active due to the loss of CPG sites. [ 3 ]

  4. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    At high temperatures, these interactions cannot form, and a functional protein is denatured. [25] However, it relies on two factors; the type of protein used and the amount of heat applied. The amount of heat applied determines whether this change in protein is permanent or if it can be transformed back to its original form. [26]

  5. Fixation (histology) - Wikipedia

    en.wikipedia.org/wiki/Fixation_(histology)

    Precipitating (or denaturing) fixatives act by reducing the solubility of protein molecules and often by disrupting the hydrophobic interactions that give many proteins their tertiary structure. The precipitation and aggregation of proteins is a very different process from the crosslinking that occurs with aldehyde fixatives.

  6. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Nucleic acids are often denatured by including urea in the buffer, while proteins are denatured using sodium dodecyl sulfate, usually as part of the SDS-PAGE process. For full denaturation of proteins, it is also necessary to reduce the covalent disulfide bonds that stabilize their tertiary and quaternary structure , a method called reducing PAGE.

  7. 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).

  8. No. 9 Alabama outlasts No. 6 Houston 85-80 in overtime at ...

    www.aol.com/no-9-alabama-outlasts-no-042326629.html

    Mark Sears scored 24 points and No. 9 Alabama beat No. 6 Houston 85-80 in overtime on Tuesday night in the opener of the Players Era Festival. After squandering an eight-point lead with 8:53 left ...

  9. Protein methods - Wikipedia

    en.wikipedia.org/wiki/Protein_methods

    Protein purification is a critical process in molecular biology and biochemistry, aimed at isolating a specific protein from a complex mixture, such as cell lysates or tissue extracts. [9] The goal is to obtain the protein in a pure form that retains its biological activity for further study, including functional assays, structural analysis, or ...