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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]
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, if any, in the supposedly unfolded state may form a folding initiation site and guide the subsequent folding reactions.
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.
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
Guanidinium thiocyanate can be used to deactivate a virus, such as the influenza virus that caused the 1918 "Spanish flu", so that it can be studied safely.. Guanidinium thiocyanate is also used to lyse cells and virus particles in RNA and DNA extractions, where its function, in addition to its lysing action, is to prevent activity of RNase enzymes and DNase enzymes by denaturing them.
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]
A chaotropic agent is a molecule in water solution that can disrupt the hydrogen bonding network between water molecules (i.e. exerts chaotropic activity).This has an effect on the stability of the native state of other molecules in the solution, mainly macromolecules (proteins, nucleic acids) by weakening the hydrophobic effect.
Limited proteolysis of a polypeptide during or after translation in protein synthesis often occurs for many proteins. This may involve removal of the N-terminal methionine, signal peptide, and/or the conversion of an inactive or non-functional protein to an active one.