Chaperone protein, molecular model

Chaperone protein, molecular model

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Credit: LAGUNA DESIGN/SCIENCE PHOTO LIBRARY

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

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