Chaperonins D018833

Chemicals and Drugs [D] » Enzymes and Coenzymes [D08] » Enzymes » Hydrolases » Acid Anhydride Hydrolases » Adenosine Triphosphatases » Chaperonins

Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Molecular Chaperones » Heat-Shock Proteins » Chaperonins

Description

A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.   MeSH

Hierarchy View

Subtype Terms (2)

Hierarchy Tree View


YOU AGREE THAT THE INFORMATION PROVIDED ON THIS WEBSITE IS PROVIDED “AS IS”, WITHOUT ANY WARRANTY OF ANY KIND, EXPRESSED OR IMPLIED, INCLUDING WITHOUT LIMITATION WARRANTIES OF MERCHANTABILITY OR FITNESS FOR ANY PARTICULAR PURPOSE, OR NON-INFRINGEMENT OF ANY THIRD-PARTY PATENT, COPYRIGHT, OR ANY OTHER THIRD-PARTY RIGHT. IN NO EVENT SHALL THE CREATORS OF THE WEBSITE OR WASHINGTON UNIVERSITY BE LIABLE FOR ANY DIRECT, INDIRECT, SPECIAL, OR CONSEQUENTIAL DAMAGES ARISING OUT OF OR IN ANY WAY CONNECTED WITH THE WEBSITE, THE USE OF THE WEBSITE, OR THIS AGREEMENT, WHETHER IN BREACH OF CONTRACT, TORT OR OTHERWISE, EVEN IF SUCH PARTY IS ADVISED OF THE POSSIBILITY OF SUCH DAMAGES.