Denaturation (biochemistry)

related topics
{acid, form, water}
{food, make, wine}
{math, number, function}

Denaturation is a process in which proteins or nucleic acids lose their tertiary structure and secondary structure 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), or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Denatured proteins can exhibit a wide range of characteristics, from loss of solubility to communal aggregation.

This concept is unrelated to denatured alcohol, which is alcohol which has been mixed with additives to make it unsuitable for human consumption.

Contents

Common examples

When food is cooked, some of its proteins become denatured. This is why boiled eggs become hard and cooked meat becomes firm.

A classic example of denaturing in proteins comes from egg whites, which are largely egg albumins in water. Fresh from the eggs, egg whites are transparent and liquid. Cooking the thermally unstable whites turns them opaque, forming an interconnected solid mass. The same transformation can be effected with a denaturing chemical. Pouring egg whites into a beaker of acetone will also turn egg whites opaque and solid. The skin which forms on curdled milk is another common example of denatured protein. The cold appetizer known as ceviche is prepared by chemically "cooking" raw fish and shellfish in an acidic citrus marinade, without heat.[1]

Full article ▸

related documents
Carbon-14
Southern blot
Pyroxene
Electron counting
Heme
Solder
Phosgene
Alcohol dehydrogenase
Borax
Ziegler-Natta catalyst
Organic acid
Nucleolus
Nuclear technology
Island of stability
Cubic zirconia
Alum
Erbium
Gel
Gel electrophoresis
Chloroform
Solvation
Beta sheet
Carbonic acid
Organelle
Neon
Neodymium
Standard electrode potential (data page)
Electrolyte
Partial pressure
Covalent bond