enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Hyperchromicity - Wikipedia

    en.wikipedia.org/wiki/Hyperchromicity

    Hyperchromicity can be used to track the condition of DNA as temperature changes. The transition/melting temperature (T m) is the temperature where the absorbance of UV light is 50% between the maximum and minimum, i.e. where 50% of the DNA is denatured. A ten fold increase of monovalent cation concentration increases the temperature by 16.6 °C.

  3. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    Denaturation can also be caused by changes in the pH which can affect the chemistry of the amino acids and their residues. The ionizable groups in amino acids are able to become ionized when changes in pH occur. A pH change to more acidic or more basic conditions can induce unfolding. [18]

  4. 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.

  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. Chevron plot - Wikipedia

    en.wikipedia.org/wiki/Chevron_plot

    A typical chevron plot observed in protein folding experiments.. A chevron plot is a way of representing protein folding kinetic data in the presence of varying concentrations of denaturant that disrupts the protein's native tertiary structure.

  7. Conformational change - Wikipedia

    en.wikipedia.org/wiki/Conformational_change

    In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. A macromolecule is usually flexible and dynamic. Its shape can change in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a ...

  8. Necrosis - Wikipedia

    en.wikipedia.org/wiki/Necrosis

    Coagulative necrosis is characterized by the formation of a gelatinous (gel-like) substance in dead tissues in which the architecture of the tissue is maintained, [7] and can be observed by light microscopy. Coagulation occurs as a result of protein denaturation, causing albumin to transform into a firm and opaque state. [6]

  9. Chromism - Wikipedia

    en.wikipedia.org/wiki/Chromism

    In chemistry, chromism is a process that induces a change, often reversible, in the colors of compounds. In most cases, chromism is based on a change in the electron states of molecules, especially the π- or d-electron state, so this phenomenon is induced by various external stimuli which can alter the electron density of substances. It is ...