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]
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
The PCR tubes are then placed in a thermal cycler to begin cycling. In the first cycle, the synthesis of cDNA occurs. The second cycle is the initial denaturation wherein reverse transcriptase is inactivated. The remaining 40-50 cycles are the amplification, which includes denaturation, annealing, and elongation.
Compared to other tests, southern blot is a complex technique that has multiple steps and these steps require equipment and reagents that are expensive. [10] High quality and large amounts of DNA are needed. [10] Southern blotting is a time consuming method and can only estimate the size of the DNA since it is a semi-quantitative method. [10]
The test was developed by Leonard Apt (1922–2013), [3] an American pediatric ophthalmologist. The test was originally used to identify the source of bloody stools in newborn infants. It has been modified to distinguish fetal from maternal hemoglobin in blood samples from any source. [4]
The process of denaturation on a denaturing gel is very sharp: "Rather than partially melting in a continuous zipper-like manner, most fragments melt in a step-wise process. Discrete portions or domains of the fragment suddenly become single-stranded within a very narrow range of denaturing conditions" (Helms, 1990).
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.
Electrophoresis refers to the electromotive force (EMF) that is used to move the molecules through the gel matrix. By placing the molecules in wells in the gel and applying an electric field, the molecules will move through the matrix at different rates, determined largely by their mass when the charge-to-mass ratio (Z) of all species is uniform.