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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. Denaturation mapping - Wikipedia

    en.wikipedia.org/wiki/Denaturation_mapping

    Denaturation Mapping is a form of optical mapping, first described in 1966. It is used to characterize DNA molecules without the need for amplification or sequencing . It is based on the differences between the melting temperatures of AT-rich and GC-rich regions. [ 1 ]

  4. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation.

  5. Denaturation - Wikipedia

    en.wikipedia.org/wiki/Denaturation

    Denaturation (biochemistry), a structural change in macromolecules caused by extreme conditions; Denaturation (fissile materials), transforming fissile materials so that they cannot be used in nuclear weapons; Denaturation (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses

  6. Helicase - Wikipedia

    en.wikipedia.org/wiki/Helicase

    This helicase was described as a "DNA unwinding enzyme" that is "found to denature DNA duplexes in an ATP-dependent reaction, without detectably degrading". [13] The first eukaryotic DNA helicase discovered was in 1978 in the lily plant. [ 14 ]

  7. Globular protein - Wikipedia

    en.wikipedia.org/wiki/Globular_protein

    Even in the protein's denatured state, it can be folded into the correct structure. Globular proteins seem to have two mechanisms for protein folding, either the diffusion-collision model or nucleation condensation model, although recent findings have shown globular proteins, such as PTP-BL PDZ2, that fold with characteristic features of both ...

  8. Polyphenol oxidase - Wikipedia

    en.wikipedia.org/wiki/Polyphenol_oxidase

    Partial denaturation actually improves hemocyanin's PPO activity by providing greater access to the active site. [47] Aureusidin synthase is homologous to plant polyphenol oxidase, but contains certain significant modifications. [citation needed] Aurone synthase [48] catalyzes the formation of aurones.

  9. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    For example, extremes of pH or temperature usually cause denaturation of all protein structure, but this is a non-specific effect. Similarly, some non-specific chemical treatments destroy protein structure: for example, heating in concentrated hydrochloric acid will hydrolyse the peptide bonds holding proteins together, releasing free amino ...