Protein denaturation
Protein Denaturation is a process in which proteins lose their tertiary structure and secondary structure which is present in their native state, by the 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. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death.
Causes of Protein Denaturation[edit | edit source]
Protein denaturation can be caused by a variety of factors, including changes in pH, temperature, ionic strength, and the concentration of polar substances. Other factors that can cause denaturation include the addition of denaturing agents such as urea, detergents, or organic solvents.
Effects of Protein Denaturation[edit | edit source]
When a protein is denatured, its secondary and tertiary structures are altered but the peptide bonds in the primary structure are not. This process is distinct from protein degradation, where the primary structure of the protein is cleaved.
Denaturation and Disease[edit | edit source]
Protein denaturation plays a role in many diseases. For example, in Alzheimer's disease, the amyloid beta protein becomes denatured and forms plaques that contribute to the disease's progression. Similarly, in Parkinson's disease, the alpha-synuclein protein becomes denatured and forms Lewy bodies, which are a hallmark of the disease.
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References[edit | edit source]
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Contributors: Prab R. Tumpati, MD