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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. Nucleic acid thermodynamics - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_thermodynamics

    The process of DNA denaturation can be used to analyze some aspects of DNA. Because cytosine / guanine base-pairing is generally stronger than adenine / thymine base-pairing, the amount of cytosine and guanine in a genome is called its GC-content and can be estimated by measuring the temperature at which the genomic DNA melts. [ 2 ]

  4. 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 ]

  5. 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]

  6. 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.

  7. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    The hyperchromic effect is the striking increase in absorbance of DNA upon denaturation. The two strands of DNA are bound together mainly by the stacking interactions, hydrogen bonds and hydrophobic effect between the complementary bases. The hydrogen bond limits the resonance of the aromatic ring so the absorbance of the sample is limited as well.

  8. The (Real) Problem With Fake Plants - AOL

    www.aol.com/real-problem-fake-plants-110123038.html

    Credit - Photo-Illustration by TIME; Capelle.r/Getty Images; Artfully79/Getty Images. W hen the German philosopher Immanuel Kant puzzled over why nature looks beautiful to us, he considered the ...

  9. Chaperone (protein) - Wikipedia

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

    The term "molecular chaperone" appeared first in the literature in 1978, and was invented by Ron Laskey to describe the ability of a nuclear protein called nucleoplasmin to prevent the aggregation of folded histone proteins with DNA during the assembly of nucleosomes. [41]