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Tethering Creates Unusual Kinetics for Ribosome-Associated Chaperones with Nascent Chains

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This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 Å 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 104 s-1 in order to keep chains unfolded.

Keywords: Chaperone; holdase; kinetic partitioning; proximity effect; ribosome-associated chaperone

Document Type: Research Article


Publication date: June 1, 2009

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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