Heat shock proteins are those functional proteins which are present in all the cells under normal conditions. But when they are exposed to high levels of temperature suddenly or some other stress like altered pH and oxygen deprivation, infection, inflammation, exercise, exposure of the cell to toxins then heat shock proteins bind to the proteins and prevent them from getting denatured.
When extreme heat is applied to proteins, chains of amino acids which constitute the proteins and are folded in spiral shape, loops and sheets begin to loose their original figures. When the interior of these proteins gets exposed which consists of hydrophobic groups, proteins can hold fast and form globs. This makes the protein dysfunctional. Such kind of dysfunctional forms of proteins can cause diseases such as Alzheimer's disease and also oncogenic transformation in humans. Left uncorrected, mis-folded proteins form aggregates that may eventually kill the cell. To prevent this happening Heat Shock Proteins are stimulated rapidly at high levels to correct this problem through transcription. Heat shock proteins are up gradated soon after a sudden stress or heat increase by heat shock factor which create heat shock response. Most heat shock proteins are called molecular chaperones. They aid in the transport of proteins throughout the cell's various compartments. They also help in the protein-protein interactions such as folding and assisting in the formation of proper protein conformation and prevention of unwanted protein aggregation. Chaperonins provide "shelters" in which new protein chains can be "incubated" until they have folded properly.
Heat shock proteins monitor the normal synthesis of proteins in the cell and help in the removal of old protein even under non stress conditions. They also function as regulators of immune response by binding antigens and presenting them to the immune system and they help in cardiovascular functioning.


• Heat Shock Proteins are classified by their molecular weight, size, structure, and function.
They are divided into several families, namely:

• HSP100

• HSP90 understanding of Hsp90 inhibitors and the molecular pathology of individual cancers will greatly contribute in identifying tumour types and individual patients will benefit most from treatment promising a healthy life. Examples of diseases that can be targeted include chronic myeloid leukaemia, melanoma, breast, ovarian, brain, thyroid, colorectal and prostate cancer.
• HSP70

• HSP60 (chaperonin)
• And small Heat Shock Proteins/ (alpha)-crystallin proteins.
Some Heat Shock Proteins, like Hsp104, have the ability to rescue already aggregated proteins.
Heat shock proteins are resistant to heat and other stress conditions because of the presence of Better Hydrogen Bonds, Better Hydrophobic Internal Packing, Enhanced Secondary Structure, Helix Dipole Stabilization.


• Heat Shock Treatment Of Cells Increases Their Survival And Resistance To Apoptosis.
• Small heat shock proteins in the production of recombinant proteins in Escherichia coli.
• The specific property of heat shock proteins helps protecting cells against injuries and other types of stress. These are also recognized by the immune system as principal antigens during infections and during the development of certain autoimmune diseases. This in turn will help in the detecting the cause of major auto immune diseases.
• Heat shock Protein can respond to stress and halt the degeneration of muscle mass caused during the body's aging process.
• When heat shock proteins (HSPs) are widely used as bio markers from in monitoring and keeping track the studies of aquatic ecosystems, this is useful to to know the specificity of synthesis of these proteins in various organisms. Bio markers are applied to endemic species and species with narrow ranges of adaptation for specific conditions in certain water bodies.

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