Web Results

en.wikipedia.org/wiki/Denaturation_(biochemistry)

Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure, and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or heat. ...

www.sciencedaily.com/terms/denaturation_(biochemistry).htm

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 ...

chemistry.elmhurst.edu/vchembook/568denaturation.html

Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process.

study.com/academy/lesson/denaturation-of-protein...

Denaturation is the process by which proteins lose their folded structure and cease to function. The Structure of Proteins: Primary Structure Before we tackle denaturation, let's look closer at ...

www.britannica.com/science/denaturation

Denaturation, in biology, process modifying the molecular structure of a protein.Denaturation involves the breaking of many of the weak linkages, or bonds (e.g., hydrogen bonds), within a protein molecule that are responsible for the highly ordered structure of the protein in its natural (native) state.Denatured proteins have a looser, more random structure; most are insoluble.

www.biology-online.org/dictionary/Denaturation

The proteins can regain their natural active state if the denaturing agent is removed. However, there are instances in which the process is irreversible. In another example, heating a double stranded DNA could lead to its denaturation as it turns into a single stranded molecule. Not all denaturation processes though lead to a change in structure.

quizlet.com/97580841/protein-denaturation-and-renaturation...

Protein Denaturation and Renaturation. STUDY. PLAY. Three things that denature a protein. Heating, pH, detergents. ... agents that increase the solubility of nonpolar residues of proteins at concentration of 5-10 M. They denature proteins by interfering with the hydrophobic interactions. Urea and guanidinium ions are two best examples.

medical-dictionary.thefreedictionary.com/Protein+denaturation

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 ...

socratic.org/questions/what-is-denaturation-and-what...

Denaturation in proteins is when a protein's secondary, tertiary, and (possibly) quaternary structures (which are held together by weak hydrogen bonds, hydrophobic interactions, etc.) are disrupted. However, the protein's primary structure remains intact (since the stronger peptide bonds are less likely to be broken).

www.britannica.com/science/protein/Protein-denaturation

Protein - Protein denaturation: When a solution of a protein is boiled, the protein frequently becomes insoluble—i.e., it is denatured—and remains insoluble even when the solution is cooled. The denaturation of the proteins of egg white by heat—as when boiling an egg—is an example of irreversible denaturation. The denatured protein has the same primary structure as the original, or ...