Chaperone protein. Molecular models of the GroEL-GroES complex chaperone protein from the bacterium Escherichia coli. It is composed of two stacked ri

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Chaperone protein. Molecular models of the GroEL-GroES complex chaperone protein from the bacterium Escherichia coli. It is composed of two stacked rings of seven GroEl proteins that form a central cavity and a GroES cap on one end. The cavity provides an enclosed environment for cellular proteins to fold themselves into their final structure. Misfolded proteins can form harmful aggregations within cells.

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Size: 5280px × 5280px
Photo credit: © LAGUNA DESIGN/SCIENCE PHOTO LIBRARY / Alamy / Afripics
License: Licensed
Model Released: No

Keywords: ., 2, artwork, bacterial, biochemical, biochemistry, cavity, chaparonin, chaperone, chemical, chemistry, coli, complex, compound, compounds, cut, cut-, cutout, duo, escherichia, folding, groel-groes, heptamer, illustration, model, molecular, molecule, molecules, pair, primary, protein, proteins, rings, stacked, structure