To combine fissionable material with nonfissionable material in order to prevent its use in an atomic weapon
to take away a natural characteristic or inherent property of a thing or a person
To subject (especially a protein) to conditions altering its original form or state
to add something that makes alcohol unsuitable for consumption but leaves the alcohol suitable for other purposes
modify (as a native protein) especially by heat, acid, alkali, or ultraviolet radiation so that all of the original properties are removed or diminished
The process of adding a substance to ethyl alcohol to make it unfit for human consumption
make (alcohol) unfit for drinking without impairing usefulness for other purposes modify (as a native protein) especially by heat, acid, alkali, or ultraviolet radiation so that all of the original properties are removed or diminished add nonfissionable material to (fissionable material) so as to make unsuitable for use in an atomic bomb
To induce structural alterations that disrupt the biological activity of a molecule Often refers to breaking hydrogen bonds between base pairs in double-stranded nucleic acid molecules to produce in single-stranded polynucleotides or altering the secondary and tertiary structure of a protein, destroying its activity
To unfold or inactivate Proteins can be denatured (e g by heat, altered pH or by chemical agents) inactivating them This process can be reversible
make (alcohol) unfit for drinking without impairing usefulness for other purposes
add nonfissionable material to (fissionable material) so as to make unsuitable for use in an atomic bomb
To change a protein from its native, functional structure to a different conformation, thereby also changing its function
The process of adding a substance to ethyl alcohol to make it unfit for human consumption; the denaturing agent may be gasoline or other substances specified by the Bureau of Alcohol, Tobacco, and Firearms
a protein is said to be denatured if it unfolds or uncoils so that its function is abolished even though the primary string of amino acids remains intact
The process of partial or total alteration of the native structure of a macromolecule resulting from the loss of tertiary or tertiary and secondary structure that is a consequence of the disruption of stabilizing weak bonds Denaturation can occur when proteins and nucleic acids are subjected to elevated temperature or to extremes of pH, or to non- physiological concentrations of salt, organic solvents, urea or other chemical agents [IUPAC Biotech]
Destruction of the natural three-dimensional structure of large biological molecules (proteins or DNA), e g through heat In the case of DNA in particular, denaturation means the dissolution of the double strand into single strands
1 The separation of the two strands of a double-stranded nucleic acid caused by treatments that overcome hydrogen bonding, e g heat 2 A usually irreversible change in the conformation of a protein caused by treatments that overcome hydrogen bonding, hydrophobic interactions, or other chemical forces that maintain the structure of proteins, e g heat
Biochemical process modifying a protein's natural configuration. It involves breaking many weak (hydrogen and hydrophobic) bonds (see bonding) that maintain the protein's highly ordered structure. This usually results in loss of biological activity (e.g., loss of an enzyme's ability to catalyze reactions). Denaturation can be brought about by heating; treatment with alkalis, acids, urea, or detergents; or even vigorous shaking of the protein solution. It can be reversed in some cases (e.g., serum albumin, hemoglobin), if conditions favourable to the protein are restored, but not in others. The term is also used to describe the process of rendering ethanol unfit to drink
1 The separation of the two strands of a double-stranded nucleic acid caused by treatments that overcome hydrogen bonding, e g , heat 2 A usually irreversible change in the conformation of a protein caused by treatments that overcome hydrogen bonding, hydrophobic interactions, or other chemical forces that maintain the structure of proteins, e g , heat
1-The changing of a protein molecule, usually by the unfolding of the chains, to a less soluble state 2-To alter the original state of a food substance by physical or chemical means
Denaturation is the loss of the native configuration of the macromolecule, such as the unfolding of the tertiary structure of an antibody protein Denaturation usually results in the loss of the macromolecule's biological or immunological reactivity or solubility
The act of making meat or left overs from being fit for human consumption Usually be treated with chemicals, some times deadly chemicals so that meat cannot be used for human consumption
A commercial term used to describe ethanol that has been rendered unfit for human consumption because of the addition of harmful ingredients to make it sales tax-expempt
Of alcohol made undrinkable, by adding a toxin or unpalatable substance, but still useful as a fuel or solvent. Traditionally by the addition of methanol (wood alcohol)