The loss of the native 3-D structure of a molecule.
A temporary or permanent change in the three-dimensional structure of a protein.
The physical changes that occur in proteins when secondary and tertiary structures are disrupted. Denaturation is usually brought about by heat treatmetnt or by a change in pH and is accompanied by a loss of biological activity.
Irreversible destruction of a macromolecule, as for example the destruction of a protein by heat.
Reversible disruption of hydrogen bonds between nucleotides converting a double-stranded DNA molecule to single-stranded molecules. Heating or strong alkali treatment result in denaturation of DNA.
disruption of the tertiary structures of a protein by agents, such as heat, pH changes, or other physical or chemical methods; as a result, the protein loses its physical and biological properties
The loss of a protein's tertiary structure. Sometimes used as a synonym of DNA melting.
The process by which a fully folded protein is unfolded by chemicals or heat. The treatment disrupts the chemical interactions between the different amino acid residues that stabilize secondary, tertiary and quaternary structure. The act of removing the disruptive treatment can often lead to renaturation of the protein.
Separation of two complementary strands of nucleic acid by breakage of the hydrogen bonds involved in base pairing. This is necessary prior to probe hybridisation and most methods involving enzymic DNA synthesis on a DNA template e.g. sequencing, PCR, some labelling methods. Denaturation may be achieved by heating or treatment with NaOH.
Changing of a protein molecule, usually by the unfolding of the chains, to a less soluble state.
A process in which a protein's structure is altered, causing the protein to become biologically inactive.
the breaking down of the three-dimensional structure of a protein, resulting in the loss of its function.
Conversion from the doublestranded to the singlestranded state, most often accomplished by heat
Separation of the two complementary DNA strands in both target DNA and labeled probe.
A condition in which a protein unfolds or its polypeptide chains are disordered, rendering the molecule less soluble and usually nonfunctional.
represents conversion of nucleic acids from the double-stranded into single-stranded forms, usually by heating or changes in pH.
Also referred to as the "melting" of DNA: the process of dividing a double-stranded DNA into two single-stranded DNAs under the influence of heat or chemicals.
the loss of the native configuration of a macromolecule resulting from heat treatment, chemical treatment, etc.; this represents the dissociation of the double helix into its complementary strands
A normally irreversible change in the structure of protein caused by heat, acid, alkali or other agents, which can result in coagulation and reduction in solubility. Denatured proteins lose biological activity but not nutritional value.
the conversion of DNA molecules from a double-stranded to a single-stranded state, most often accomplished by heating.
describes the conversion of DNA from the double-stranded to the single-stranded state; separation of the strands is most often accomplished by heating.
A process pertaining to a change in structure of a protein form regular to irregular arrangement of the polypeptide chains.
The separation of the two strands of a DNA double helix or the severe disruption of the structure of any complex molecule without breaking the major bonds of its chains.
Addition of methanol or acetone to alcohol to make it unfit for drinking Change in molecular structure of proteins so that they cannot function normally, often caused by splitting of hydrogen bonds following exposure to reactive substances or heat
the alteration of a protein's three-dimensional structure.
the process of splitting the complementary double strands of DNA to form single strands
Drastic alteration in the conformation of a protein or nucleic acid due to disruption of various noncovalent bonds caused by heating or exposure to certain chemicals; usually results in loss of biological function.
Denaturation is the alteration of a protein shape through some form of external stress (for example, by applying heat, acid or alkali), in such a way that it will no longer be able to carry out its cellular function. Denatured proteins can exhibit a wide range of characteristics, from loss of solubility to communal aggregation.
