Chaperonin protein complex

Chaperonin protein complex

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Credit: LAGUNA DESIGN/SCIENCE PHOTO LIBRARY

Caption: Chaperonin protein complex. Molecular model of the chaperonin GroEL from the bacteria Escherichia coli complexed with capsid assembly protein gp31 from the enterobacteria phage T4. Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation (clumping) due to mis-folded proteins. Here the phage is using the bacteria's chaperonin protein to assemble new viruses after infecting the cell and replicating.

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Keywords: artwork, bacterial, bacteriphage t4, biochemical, biochemistry, biological, biology, capsid assembly protein, chaperonin, complex, cut out, cut outs, cut-out, cut-outs, cutout, cutouts, e coli, escherichia coli, gp31, groel, illustration, microbiological, microbiology, molecular model, molecule, protein, proteomics, space fill, space filled, space-fill, space-filled, structure, viral, white background

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