denaturation

Biology

(noun)

the change of folding structure of a protein (and thus of physical properties) caused by heating, changes in pH, or exposure to certain chemicals

Related Terms

  • chaperonin
  • polymerase chain reaction
  • electrophoresis
Physiology

(noun)

Denaturation is a process in which proteins or nucleic acids lose their tertiary and secondary structure which is present in their native state, by 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), or heat.

Related Terms

  • protein
  • amino acid

Examples of denaturation in the following topics:

  • Denaturation and Protein Folding

    • Denaturation is a process in which proteins lose their shape and, therefore, their function because of changes in pH or temperature.
    • The stomach maintains a very low pH to ensure that pepsin continues to digest protein and does not denature.
    • However, denaturation can be irreversible in extreme situations, like frying an egg.
    • The heat from a pan denatures the albumin protein in the liquid egg white and it becomes insoluble.
    • The protein in meat also denatures and becomes firm when cooked.
  • Protein Folding, Modification, and Targeting

    • When a protein loses its biological function as a result of a loss of three-dimensional structure, we say that the protein has undergone denaturation.
    • Proteins can be denatured not only by heat, but also by extremes of pH; these two conditions affect the weak interactions and the hydrogen bonds that are responsible for a protein's three-dimensional structure.
    • The denatured state of the protein does not equate with the unfolding of the protein and randomization of conformation.
    • Actually, denatured proteins exist in a set of partially-folded states that are currently poorly understood.
  • DNA Sequencing Based on Sanger Dideoxynucleotides

    • Following rounds of template DNA extension from the bound primer, the resulting DNA fragments are heat denatured and separated by size using gel electrophoresis.
    • This is frequently performed using a denaturing polyacrylamide-urea gel with each of the four reactions run in one of four individual lanes (lanes A, T, G, C).
  • Peptide Synthesis

    • This denaturation is often done deliberately in the course of separating and purifying proteins.
    • Some treatments known to denature proteins are listed in the following table.
    • Not all proteins are easily denatured.
    • Although globular proteins are generally sensitive to denaturation (structural unfolding), some can be remarkably stable.
    • One procedure for purifying it involves treatment with a hot sulfuric acid solution, which denatures and partially decomposes most proteins other than ribonuclease A.
  • Western Blots

    • The technique uses gel electrophoresis to separate native proteins by 3-D structure or denatured proteins by the length of the polypeptide.
  • The Role of the Kidneys in Acid-Base Balance

    • Outside the range, pH becomes incompatible with life; proteins are denatured and digested, enzymes lose their ability to function, and the body is unable to sustain itself.
  • Amplifying DNA: The Polymerase Chain Reaction

    • Denaturation step: This step is the first regular cycling event and consists of heating the reaction to 94-98 °C.
    • Denaturing at 96°C. 2.
  • Fever

    • Fever is normally beneficial immune process, because increased body temperature can kill off bacteria and viruses, and denature bacterial enzymes, however it is not helpful in every case.
    • High fevers will also denature the bodies own proteins, which can alter normal cell metabolism, and lead to cell injury and death.
  • Chemical Buffer Systems

    • Outside the acceptable range of pH, proteins are denatured and digested, enzymes lose their ability to function, and death may occur.
  • High Pressure

    • In the process, the food's proteins are denatured, hydrogen bonds are fortified, and noncovalent bonds in the food are disrupted, while the product's main structure remains intact.
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