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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. Anfinsen's dogma - Wikipedia

    en.wikipedia.org/wiki/Anfinsen's_dogma

    Folded, 3-D structure of ribonuclease A. Anfinsen's dogma, also known as the thermodynamic hypothesis, is a postulate in molecular biology.It states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence. [1]

  4. Christian B. Anfinsen - Wikipedia

    en.wikipedia.org/wiki/Christian_B._Anfinsen

    Christian Boehmer Anfinsen Jr. (March 26, 1916 – May 14, 1995) [1] was an American biochemist.He shared the 1972 Nobel Prize in Chemistry with Stanford Moore and William Howard Stein for work on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation (see Anfinsen's dogma).

  5. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Many allergies are caused by the incorrect folding of some proteins because the immune system does not produce the antibodies for certain protein structures. [5] 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 ...

  6. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    This model tries to answer the question of whether the denaturant molecules actually bind to the protein or they seem to be bound just because denaturants occupy about 20-30% of the total solution volume at high concentrations used in experiments, i.e. non-specific effects – and hence the term ‘weak binding’. As in the denaturant-binding ...

  7. Chaperone (protein) - Wikipedia

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

    Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. [5] The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria.

  8. US Park Police officer won't be charged in shooting death of ...

    www.aol.com/news/us-park-police-officer-wont...

    A U.S. Park Police officer who fatally shot a 17-year-old boy after getting into a car being driven by the young man will not face charges, according to the U.S. Attorney’s Office for the ...

  9. Nucleic acid thermodynamics - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_thermodynamics

    The term is also often used to describe the reformation (renaturation) of reverse-complementary strands that were separated by heat (thermally denatured). Proteins such as RAD52 can help DNA anneal. DNA strand annealing is a key step in pathways of homologous recombination.