Chaperonin: Difference between revisions
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<StructureSection load='1pcq' size='350' side='right' caption='E. coli GroEL/GroES complex with ADP, AlF3, Mg+2 and K+ ions (PDB entry [[1pcq]])' scene='44/445432/Cv/1'> | <StructureSection load='1pcq' size='350' side='right' caption='E. coli GroEL green)/GroES (magenta) complex with ADP, AlF3, Mg+2 and K+ ions (PDB entry [[1pcq]])' scene='44/445432/Cv/1'> | ||
[[Image:1pcq.png|left|200px|thumb|Crystal Structure of Chaperonin, [[1pcq]]]] | [[Image:1pcq.png|left|200px|thumb|Crystal Structure of Chaperonin, [[1pcq]]]] | ||
'''Chaperonins''' (CPN) are oligomeric proteins that mediate the folding of polypeptide chains. '''Group I CPN''' are found in bacteria, chloroplasts and mitochondria. For an introductory overview, see [http://en.wikipedia.org/wiki/Chaperonins Chaperonins in Wikipedia]. | '''Chaperonins''' (CPN) are oligomeric proteins that mediate the folding of polypeptide chains. '''Group I CPN''' are found in bacteria, chloroplasts and mitochondria. For an introductory overview, see [http://en.wikipedia.org/wiki/Chaperonins Chaperonins in Wikipedia]. | ||
