Chaperones: Difference between revisions
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<StructureSection load=' | <StructureSection load='4JN4' size='340' side='right' caption='' scene=''> | ||
Chaperones are proteins that are involved in the non-covalent folding and unfolding of other macromolecules. It exists both in prokaryotes and eukaryotes. Some chaperones are constitutively expressed in the system however, there are other chaperones that are expressed only in response to an external stimulus or stress such as heat and therefore they are referred to as ''heat shock proteins''.They are classified based on their structure, size, molecular weight and function in to several classes such as Hsp100, Hsp90, Hsp60 (chaperonins) [http://proteopedia.org/wiki/index.php/Chaperonin], small heat shock proteins (alpha)-crystallin proteins. They do not undergo denaturation themselves when exposed to stress because of better hydrogen bonding, strong hydrophobic core interactions, enhanced secondary structure and helix dipole stabilization. | Chaperones are proteins that are involved in the non-covalent folding and unfolding of other macromolecules. It exists both in prokaryotes and eukaryotes. Some chaperones are constitutively expressed in the system however, there are other chaperones that are expressed only in response to an external stimulus or stress such as heat and therefore they are referred to as ''heat shock proteins''.They are classified based on their structure, size, molecular weight and function in to several classes such as Hsp100, Hsp90, Hsp60 (chaperonins) [http://proteopedia.org/wiki/index.php/Chaperonin], small heat shock proteins (alpha)-crystallin proteins. They do not undergo denaturation themselves when exposed to stress because of better hydrogen bonding, strong hydrophobic core interactions, enhanced secondary structure and helix dipole stabilization. | ||
== Function == | == Function == | ||