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denaturation
(redirected from Protein denaturation)

   Also found in: Encyclopedia, Wikipedia 0.01 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 yogurt manufacture, milk undergoes a very high heat treatment to cause whey protein denaturation and its association with casein micelles.
To assess protein stability in field collected organisms at a proteome scale, we developed a high-throughput assay for protein denaturation profiles of total tissue extracts in bivalves.
This occurs because of the higher activation energy of meat protein denaturation, compared with the lower activation energy of disrupting the most vulnerable bacterial enzymes.
 
 
 
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