Heat shock protein: Difference between revisions
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Heat-shock proteins (hsp) are synthesised in response to increased levels of [[Protein folding|misfolded proteins]], especially after a cell being exposed to heat or other kind of stress. Being a type of [[Molecular chaperone|molecular chaperone]], heat-shock proteins bind to misfolded proteins, eventually release them and allow refolding<ref>Alberts, B. Johnson, A. Lewis, J. (2015). Molecular biology of the cell. 6th ed. New York: Garland Science, Chapter 6, page 355.</ref>. | Heat-shock proteins (hsp) are synthesised in response to increased levels of [[Protein folding|misfolded proteins]], especially after a cell being exposed to heat or other kind of stress. Being a type of [[Molecular chaperone|molecular chaperone]], heat-shock proteins bind to misfolded proteins, eventually release them and allow refolding<ref>Alberts, B. Johnson, A. Lewis, J. (2015). Molecular biology of the cell. 6th ed. New York: Garland Science, Chapter 6, page 355.</ref>.<br> | ||
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Latest revision as of 17:50, 22 October 2018
Heat-shock proteins (hsp) are synthesised in response to increased levels of misfolded proteins, especially after a cell being exposed to heat or other kind of stress. Being a type of molecular chaperone, heat-shock proteins bind to misfolded proteins, eventually release them and allow refolding[1].
Reference
- ↑ Alberts, B. Johnson, A. Lewis, J. (2015). Molecular biology of the cell. 6th ed. New York: Garland Science, Chapter 6, page 355.