renaturation


Also found in: Dictionary, Encyclopedia, Wikipedia.

re·na·tu·ra·tion

(rē'nā-tyū-rā'shŭn),
The conversion of a denatured and inactive macromolecule back to its natured and bioactive configuration.

renaturation

(rē-nā′chər-ā′shən)
n.
The process by which proteins or complementary strands of nucleic acids re-form their native conformations.

re·na′ture v.

renaturation

(rē″nā″chŭ-rā′shŏn) [ re- + (de)naturation]
The reassembly of a molecule or the shape of a molecule, e.g., the rejoining of unraveled complementary strands of DNA into a double helix.
renature (rē-nā′chŭr) renatured (rē-nā′chŭrd)

renaturation

the reassembly of a protein or nucleic acid molecule after denaturation.
References in periodicals archive ?
Expression, purification and renaturation of truncated human integrin b1 from inclusion bodies of Escherichia coli.
Cloning, expression, and renaturation studies of reteplase.
By renaturation after denaturation, it is found that the a-amylase activity with higher DE dextrin as carbon source was still higher than that of lower DE dextrin.
Brown coal surface-mining sites of the former German Democratic Republic undergo extensive renaturation, thus providing new biotopes for many plant and animal species, including ticks.
Fusing DNA Strands: If the heated solution is cooled down, the separated strands fuse within the hydrogen bonds (this cooling down must be done slowly so that the corresponding complementary bases have enough time to find each other), called renaturation.
The potential damaging effects of reactive oxygen species can be partially reversed by molecular chaperones, such as heat shock protein 27 (Hsp27) that may be involved in a process of protein renaturation (Ferns et al.
Zinc in p53 structural stabilization and functional activation: Zinc has been shown to be responsible for the functional conformation of the tumour suppressor p53 protein (52) and the addition of the physiologic zinc concentrations was seen to mediate the renaturation of wild type p53 (53).
At a low concentration of primers or in their absence, there is an equal probability of formation of homo or heteroduplexes upon renaturation.
This will have to remain in the realm of prediction, as I cannot find any reference to the blackbody radiation spectrum of folding simple proteins as the temperature falls below the renaturation temperature.
Their functions, based on amino acid sequences, have been proposed to include: renaturation of unfolded proteins, protection of proteins from denaturing, protection of membranes, and sequestration of ions (Bray, 1993).