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Heat Shock Proteins (Hsps) are a specific group of chaperone proteins whose expression is increased upon exposure to elevated temperatures or stress.
Hsps exist in all organisms and are highly conserved. They are also commonly known as 'stress proteins' and are divided into several families according to their molecular weights.
Unlike other proteins Hsps do not denature under conditions of stress as they have better hydrophobic packing, enhanced secondary protein structure, stronger hydrogen bonds and helix dipole stabilization. Instead, Hsps act to protect other cellular proteins from thermal or oxidative stress, which can cause protein unfolding, conformational changes in the protein structure and aggregation, potentially leading to a variety of pathologies. To do this, Hsps act as 'molecular chaperones' and are able to stabilize and assist in the folding of substrate proteins to the native state. Some Hsps also direct denatured proteins to the proteasome for their proteolytic destruction during the heat shock response.