This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Chaperonin
From Proteopedia
Michal Harel (Talk | contribs)
(New page: Crystal Structure of Chaperonin, 1svt {{STRUCTURE_1svt| PDB=1svt | SIZE=300| SCENE= |right|CAPTION=GroEL/GroES complex, 1svt }} Chaperonin (C...)
Next diff →
Revision as of 07:46, 21 April 2011
Chaperonin (CPN) are oligomeric proteins which mediate the folding of polypeptide chains. Group I CPNs are found in bacteria, chloroplasts and mitochondria. They include the most characterized GroEL/GroES complex from Escherichia coli and CPN60/CPN10 from Thermus thermophilus. The larger subunit (GroEL, CPN60) contains 3 domains. The apical domain is the one which binds the substrate. Group II CPNs are found in eukaryotic cytosol and archaea. Thermosome is a CPN complex found in archaea. CCT is a CPN complex found in eukarya.
Contents |
3D Structures of Chaperonin
[Category:Topic Page]]
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Eric Martz, Jaime Prilusky
