Tethering creates unusual kinetics for ribosome-associated chaperones with nascent chains.

Protein Pept. Lett.2009;16(6):631-4. doi:10.2174/092986609788490195

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This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 A from the emerging nascent chain has an effective concentration of 1 x 10(-1) M, which is 4-5 orders of magnitude larger than the concentration of the chaperone in the cytosol. Ribosome-bound chaperones bind nascent chains intramolecularly with rates as large as 10(4) s(-1) in order to keep chains unfolded.

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Tethering creates unusual kinetics for ribosome-associated chaperones with nascent chains.

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