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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. 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.

  4. Extremozyme - Wikipedia

    en.wikipedia.org/wiki/Extremozyme

    An extremozyme is an enzyme, often created by archaea, which are known prokaryotic extremophiles that can function under extreme environments. Examples of such are those in highly acidic/basic conditions, high/low temperatures, high salinity, or other factors, that would otherwise denature typical enzymes (e.g. catalase, rubisco, carbonic anhydrase). [1]

  5. Renal physiology - Wikipedia

    en.wikipedia.org/wiki/Renal_physiology

    Outside the range of pH that is compatible with life, proteins are denatured and digested, enzymes lose their ability to function, and the body is unable to sustain itself. The kidneys maintain acid-base homeostasis by regulating the pH of the blood plasma. Gains and losses of acid and base must be balanced.

  6. DNA unwinding element - Wikipedia

    en.wikipedia.org/wiki/DNA_unwinding_element

    DUE-B's are 209 residues in total, 58 of which are disordered until bound to DUE. [3] DUE-B's hydrolyze ATP In order to function. [3] Also possess similar sequence to aminoacyl-tRNA synthetase, and were previously classified a such. [13] DUE-Bs form homodimers that create an extended beta-sheet secondary structure extending across it. [3]

  7. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Exopeptidase enzymes exist in the small intestine. These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. They are present in all lifeforms and are crucial for survival since they do many ...

  8. 4 ways pineapple can improve your love life - AOL

    www.aol.com/4-ways-pineapple-improve-love...

    It's also worth noting that pineapple can interact with certain medications—and that's largely due to good ol' bromelain. The enzyme is known to raise the risk of or cause unwanted interactions ...

  9. dnaB helicase - Wikipedia

    en.wikipedia.org/wiki/DnaB_helicase

    DnaB helicase is an enzyme in bacteria which opens the replication fork during DNA replication.Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. [1]

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