Foldase
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In
molecular biology Molecular biology is the branch of biology that seeks to understand the molecule, molecular basis of biological activity in and between Cell (biology), cells, including biomolecule, molecular synthesis, modification, mechanisms, and interactions ...
, foldases are a particular kind of
molecular chaperones Chaperone proteins participate in the folding of over half of all mammalian proteins. In molecular biology, molecular chaperones are protein Proteins are large biomolecules or macromolecules that are comprised of one or more long chains of amin ...
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 Chaperone (protein), molecular chaperones, and is found in many bacteria. It is required for the proper protein folding, folding of many proteins. To function properly, GroEL requires th ...

GroEL
/ GroES and the
DnaK The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family In human society, family (from la, familia) is a group of people related either by consanguinity (by recognized birth) or affinity (by marriage or other relationship). T ...
/
DnaJ In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock proteinHeat shock proteins (HSP) are a family of proteins that are produced by cells in response to exposure to stressful conditions. They were first described in relation to ...
/
GrpEGrpE (''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 protei ...
system.


References

{{reflist http://www.embl.de/pepcore/pepcore_services/protein_expression/ecoli/improving_protein_solubility/


See also

* Holdase * Chaperonin * Co-chaperone Molecular chaperones Protein biosynthesis