denaturation


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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.

de·na·tur·a·tion

(dē-na'tyū-rā'shŭn),
The process of becoming denatured.

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.

de·na·tur·a·tion

(dē-nā'chŭr-ā'shŭn)
The process of becoming denatured.

denaturation

1. Alteration in the folding pattern of a protein by heat or chemical reaction from its physiological conformation to an inactive shape.
2. In the case of DNA or RNA the conversion from a double-stranded structure to a single stranded structure, usually by heating. This is an essential stage in the POLYMERASE CHAIN REACTION.

denaturation

the breakdown of the bonds forming the quaternary, tertiary and secondary structures of PROTEINS and NUCLEIC ACIDS, a process that can be caused by various agents, such as excess heat, strong acids or alkalis, organic solvents and ultrasonic vibration. In some cases, denaturation is irreversible as in, for example, the heating of egg albumen to give solid egg white. When denaturation occurs in enzymes, they are inactivated, with major effects in living organisms. Denatured nucleic acids can often be returned to their original configuration in the process of renaturation.

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.
References in periodicals archive ?
Therefore, the increase in MCTs in the LD muscle of summer stressed Ghungroo pigs, as observed in the present study, may be advantageous for maintaining pH regulation and muscle acidification by efficient efflux of mono-carboxylates out of muscle, such as lactate, which could have subsequently led to reduced drip loss and protein denaturation.
Denaturation is a process in which proteins lose the tertiary structure and secondary structure which is present in their native state, Thermodynamics and activation parameters provide a detailed mechanism for many chemical and biological reactions [41].
Repeating cycles of helicase denaturation, primer annealing, and polymerase extension act very much like classical PCR at this point, resulting in large-scale production of a primer-to-primer DNA product (Figure 2e) in those reactions where a template matching the primers existed.
Initially, fresh DNA polymerase had to be added after each denaturation step.
One of the storage proteins of soybeans has been reported to undergo reversible dissociation and denaturation at 2[degrees]C [19].
They attributed such impact to denaturation of whey proteins that co-precipitated with the caseins.
MPS may affect the tear film components by impacting the protein denaturisation process and subsequent deposition on contact lenses A recent in vitro study investigated the ability of a novel B&L investigative multi purpose (MPS) solutions and four commercially available MPS to stabilise a protein (lysozyme) from denaturation.
The amplifications were made by one initial denaturation cycle for 5 min at 95[degrees]C, 35 cycles of denaturation at 95[degrees]C for 1 min, annealing at 62[degrees]C for 1 min, and extension at 72[degrees]C for 1 min.
The temperature cycling conditions of amplification were as follows: PPAR[gamma], an initial step of 45 [degrees]C for 20 min, denaturation at 94 [degrees]C for 3 min, 30 cycles of denaturation at 94 [degrees]C for 1 min, annealing at 55 [degrees]C for 1 min, and elongation at 72 [degrees]C for 1 min, and a final extension at 72 [degrees]C for 8 min.
Researchers can use the software to genotype samples based on the thermal denaturation properties of double-stranded DNA.
Each isolate was then identified to the genus level by amplification with genus specific primer LbLMA-rev (5' CTC AAA ACT AAA CAAAGT TTC 3') and a universal primer R16-1 (5' CTT GTA CAC ACC GCC CGT TCA 3') using programme as initial denaturation at 94[degrees]C for 5 min, followed by 30 cycles of denaturation at 94[degrees]C for 30 sec, annealing at 55[degrees]C and extension at 72[degrees]C for 30 sec and 7 min thereafter (7).