Chaperonin: Difference between revisions

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<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'>
<StructureSection load='' 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].