Search results
Results from the WOW.Com Content Network
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]
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]
Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]
Cleavage of fusion protein so that the fusion partner and protein tag used in protein expression and purification may be removed. The proteases used have high degree of specificity, such as thrombin , enterokinase , and TEV protease , so that only the targeted sequence may be cleaved.
Tandem repeats are unstable regions of the genome where frequent insertions and deletions of nucleotides can take place, resulting in genome rearrangements. [3] DNA polymerase , the main enzyme to catalyze the polymerization of free deoxyribonucleotides into a newly forming DNA strand, plays a significant role in the occurrence of this mutation.
Proteins are highly susceptible to denaturation due to environmental conditions and organisms that live in hazardous conditions should have a basal level of HSP expression. [1] However, other adaptations, such as colonizing less hazardous microhabitats or other behavioral adaptations, could also contribute to acclimation in stressful habitats.
Melting curve analysis is an assessment of the dissociation characteristics of double-stranded DNA during heating. As the temperature is raised, the double strand begins to dissociate leading to a rise in the absorbance intensity, hyperchromicity.
Denaturation midpoint of a protein is defined as the temperature (T m) or concentration of denaturant (C m) at which both the folded and unfolded states are equally populated at equilibrium (assuming two-state protein folding). T m is often determined using a thermal shift assay.