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denaturation
(redirected from Denaturating)

   Also found in: Encyclopedia, Wikipedia 0.03 sec.
denaturation /de·na·tur·a·tion/ (de-na″cher-a´shun) destruction of the usual nature of a substance, as by the addition of methanol or acetone to alcohol to render it unfit for drinking, or the change in the physical properties of a substance, as a protein or nucleic acid, caused by heat or certain chemicals that alter tertiary structure.
denaturation
[dēnā′chərā′shən]
Etymology: L, de + natura, natural
1 the alteration of the basic nature or structure of a substance.
2 the process of making a potential food or beverage substance unfit for human consumption although it may still be used for other purposes, such as a solvent.

denaturation [de-na″chur-a´shun]
a change in the usual nature of a substance, as by the addition of methanol or acetone to alcohol to render it unfit for drinking, or the change in the physical properties of a substance, such as a protein or nucleic acid, caused by heat or certain chemicals that alter tertiary structure.
protein denaturation any nonproteolytic change in the chemistry, composition, or structure of a native protein that causes it to lose some or all of its unique or specific characteristics.

denaturation
1. a change in the usual nature of a substance, as by the addition of methanol or acetone to alcohol to render it unfit for drinking.
2. in proteins and nucleic acids produced by heat or certain chemicals, usually results in loss of function. In proteins, various noncovalent bonds are disrupted resulting in unfolding of the polypeptide chain; in nucleic acids hydrogen bonds between nucleotides are disrupted converting double-stranded molecules or parts of them into single-stranded forms.

protein denaturation
any nonproteolytic change in the chemistry, composition or structure of a native protein which causes it to lose some or all of its unique or specific characteristics.


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In addition, we tested the application of denaturating high-performance liquid chromatography (DHPLC) for the identification of the ITS PCR product to distinguish M.
Effects and agents driving and facilitating the thiol/disulfide exchange reaction are higher temperature, denaturating agents like SDS, chaotropic ions, and basic conditions.
Cytoskeletal proteins were separated by 10% SDS-polyacrylamide gel electrophoresis, under denaturating conditions, and then transferred to Immobilion-P (Millipore, Bedford, MA, USA) membranes.
 
 
 
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