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September 03, 2010

Volume 285Issue 36p27499-28398, e11-e13, e99964-e99965
Open Access
On The Cover: Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. The cover figure shows the first crystal structure of a group II chaperonin in an open conformation. We have obtained structures of the archaeal chaperonin from Methanococcus maripaludis in both a peptide acceptor (open) state and a protein folding (closed) state. For details see the article by Pereira et al., pages 27958–27966....
On The Cover: Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. The cover figure shows the first crystal structure of a group II chaperonin in an open conformation. We have obtained structures of the archaeal chaperonin from Methanococcus maripaludis in both a peptide acceptor (open) state and a protein folding (closed) state. For details see the article by Pereira et al., pages 27958–27966.

Papers of the Week

Minireviews

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Glycobiology and Extracellular Matrices

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Membrane Biology

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Microbiology

Molecular Bases of Disease

Molecular Biophysics

Neurobiology

Protein Structure and Folding

Protein Synthesis and Degradation

RNA

Signal Transduction

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