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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.
Protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1 MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner.
Chaperonins are a class of molecular chaperone composed of oligomeric double-ring protein assemblies that provide essential kinetic assistance to protein folding by binding non-native proteins and allowing them to fold in the central cavities of their rings.
Chaperonins are large barrel-like complexes that facilitate protein folding by encapsulating individual unfolded polypeptides so they can fold properly and attain the native conformation. Two groups of chaperonins exist.
Hsp60 (heat shock proteins of the 60 kDa size) family members are also known as chaperonins. There are two classes of chaperonins based on sequence homology and the requirement of an additional subunit that functions as a regulatory lid (Kusmierczyk & Martin, 2001).
7 Ιουλ 1998 · The chaperonins are large, double-ring oligomeric proteins that act as containers for the folding of other protein subunits. Together with its co-protein GroES, GroEL binds non-native polypeptides and facilitates their refolding in an ATP-dependent manner.
20 Μαΐ 1999 · As their name suggests, molecular chaperones are there to ensure the right molecules meet and that nothing untoward happens when they do. The chaperonins themselves fall into two subfamilies: the GroE subfamily (or Group I chaperonins) and the TCP-1 subfamily (or Group II chaperonins).
