Chaperonin: Difference between revisions
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[[Image:1pcq.png|left|200px|thumb|Crystal Structure of Chaperonin, [[1pcq]]]] | [[Image:1pcq.png|left|200px|thumb|Crystal Structure of Chaperonin, [[1pcq]]]] | ||
{{STRUCTURE_1pcq| PDB=1pcq | SIZE=400| SCENE=Chaperonin/Groel_groes_comnplex/1 |right|CAPTION=GroEL/GroES complex, [[1pcq]] }} | {{STRUCTURE_1pcq| PDB=1pcq | SIZE=400| SCENE=Chaperonin/Groel_groes_comnplex/1 |right|CAPTION=GroEL/GroES complex, [[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]. | ||