In
molecular biology
Molecular biology is the branch of biology that seeks to understand the molecular basis of biological activity in and between cells, including biomolecular synthesis, modification, mechanisms, and interactions. The study of chemical and physi ...
, foldases are a particular kind of
molecular chaperones
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to ass ...
that assist the non-covalent folding of proteins in an ATP-dependent manner.
Examples of foldase systems are the
GroEL
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein com ...
/
GroES
Heat shock 10 kDa protein 1 (Hsp10), also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF), is a protein that in humans is encoded by the ''HSPE1'' gene. The homolog in '' E. coli'' is GroES that is a chaperonin which usually works ...
and the
DnaK
The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms. Intracellularly localized Hsp70s are an importa ...
/
DnaJ
In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein. It is expressed in a wide variety of organisms from bacteria to humans.
Function
Molecular chaperones are a diverse family o ...
/
GrpE GrpE (''Gro-P'' like protein E) is a bacterial nucleotide exchange factor that is important for regulation of protein folding machinery, as well as the heat shock response. It is a heat-inducible protein and during stress it prevents unfolded prote ...
system.
References
{{reflist
http://www.embl.de/pepcore/pepcore_services/protein_expression/ecoli/improving_protein_solubility/
See also
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Holdase In molecular biology, holdases are a particular kind of molecular chaperones that assist the non-covalent folding of proteins in an ATP-independent manner. Examples of holdases are DnaJ and Hsp33.
Holdases bind to protein folding intermediates to ...
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Chaperonin
HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 bel ...
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Co-chaperone
Co-chaperones are proteins that assist chaperones in protein folding and other functions. Co-chaperones are the non-client binding molecules that assist in protein folding mediated by Hsp70 and Hsp90. They are particularly essential in stimulation ...
Molecular chaperones
Protein biosynthesis