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• Cryo-EM structures of GroEL:ES2 with RuBisCO visualize molecular

Cryo-EM structures of GroEL:ES2 with RuBisCO visualize molecular

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Cryo-EM structures of GroEL:ES2 with RuBisCO visualize molecular

Structural basis of substrate progression through the bacterial

Single-particle cryo-EM analysis of the shell architecture and

GroEL Ring Separation and Exchange in the Chaperonin Reaction

Schematic of the GroEL-GroES reaction cycle. (1) A non-native

Cycling GroEL-GroES can fold PepQ faster than confinement alone

GroEL Ring Separation and Exchange in the Chaperonin Reaction

The GroEL C-termini helps retain and unfold the PepQ monomer. (a,b

Cryo-EM maps and Cα atom model derived from 4.5 to 3.88 Å

Subunit conformational variation within individual GroEL oligomers

Single-particle cryo-EM analysis of the shell architecture and

Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein